PubMed:26692049 JSONTXT

{"project":"GlyCosmos6-UBERON","denotations":[{"id":"T1","span":{"begin":104,"end":111},"obj":"Body_part"},{"id":"T2","span":{"begin":169,"end":177},"obj":"Body_part"},{"id":"T3","span":{"begin":208,"end":215},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0031975"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0031975"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0004529"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":586,"end":593},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":606,"end":613},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":586,"end":593},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":606,"end":613},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":140},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":141,"end":262},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":263,"end":482},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":483,"end":636},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":637,"end":825},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":826,"end":949},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":950,"end":1074},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1075,"end":1281},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1282,"end":1402},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":140},"obj":"Sentence"},{"id":"T2","span":{"begin":141,"end":262},"obj":"Sentence"},{"id":"T3","span":{"begin":263,"end":482},"obj":"Sentence"},{"id":"T4","span":{"begin":483,"end":636},"obj":"Sentence"},{"id":"T5","span":{"begin":637,"end":825},"obj":"Sentence"},{"id":"T6","span":{"begin":826,"end":949},"obj":"Sentence"},{"id":"T7","span":{"begin":950,"end":1074},"obj":"Sentence"},{"id":"T8","span":{"begin":1075,"end":1281},"obj":"Sentence"},{"id":"T9","span":{"begin":1282,"end":1402},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":140},"obj":"Sentence"},{"id":"T2","span":{"begin":141,"end":262},"obj":"Sentence"},{"id":"T3","span":{"begin":263,"end":482},"obj":"Sentence"},{"id":"T4","span":{"begin":483,"end":636},"obj":"Sentence"},{"id":"T5","span":{"begin":637,"end":825},"obj":"Sentence"},{"id":"T6","span":{"begin":826,"end":949},"obj":"Sentence"},{"id":"T7","span":{"begin":950,"end":1074},"obj":"Sentence"},{"id":"T8","span":{"begin":1075,"end":1281},"obj":"Sentence"},{"id":"T9","span":{"begin":1282,"end":1402},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":586,"end":593},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":606,"end":613},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":84,"end":92},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":288,"end":299},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:1163"},{"id":"A2","pred":"db_id","subj":"T2","obj":"NCBItxid:1167"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":308,"end":311},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0004974"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0022673"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":112,"end":126},"obj":"FMAID:82785"},{"id":"_T2","span":{"begin":112,"end":126},"obj":"FMAID:196779"},{"id":"_T3","span":{"begin":112,"end":126},"obj":"FMAID:196735"},{"id":"_T4","span":{"begin":112,"end":126},"obj":"FMAID:82746"},{"id":"_T5","span":{"begin":178,"end":192},"obj":"FMAID:196735"},{"id":"_T6","span":{"begin":178,"end":192},"obj":"FMAID:196779"},{"id":"_T7","span":{"begin":178,"end":192},"obj":"FMAID:82746"},{"id":"_T8","span":{"begin":178,"end":192},"obj":"FMAID:82785"},{"id":"_T9","span":{"begin":336,"end":340},"obj":"FMAID:198663"},{"id":"_T10","span":{"begin":336,"end":348},"obj":"FMAID:198017"},{"id":"_T11","span":{"begin":336,"end":348},"obj":"FMAID:84082"},{"id":"_T12","span":{"begin":436,"end":444},"obj":"FMAID:165447"},{"id":"_T13","span":{"begin":436,"end":444},"obj":"FMAID:67257"},{"id":"_T14","span":{"begin":586,"end":593},"obj":"FMAID:196732"},{"id":"_T15","span":{"begin":586,"end":593},"obj":"FMAID:82743"},{"id":"_T16","span":{"begin":606,"end":613},"obj":"FMAID:82743"},{"id":"_T17","span":{"begin":606,"end":613},"obj":"FMAID:196732"},{"id":"_T18","span":{"begin":937,"end":942},"obj":"FMAID:196724"},{"id":"_T19","span":{"begin":1040,"end":1045},"obj":"FMAID:196724"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":194,"end":197},"obj":"http://www.uniprot.org/uniprot/Q9Y251"},{"id":"T2","span":{"begin":281,"end":284},"obj":"http://www.uniprot.org/uniprot/Q9Y251"},{"id":"T3","span":{"begin":356,"end":359},"obj":"http://www.uniprot.org/uniprot/Q9Y251"},{"id":"T4","span":{"begin":1377,"end":1380},"obj":"http://www.uniprot.org/uniprot/Q9Y251"},{"id":"T5","span":{"begin":194,"end":197},"obj":"http://www.uniprot.org/uniprot/O15197"},{"id":"T6","span":{"begin":281,"end":284},"obj":"http://www.uniprot.org/uniprot/O15197"},{"id":"T7","span":{"begin":356,"end":359},"obj":"http://www.uniprot.org/uniprot/O15197"},{"id":"T8","span":{"begin":1377,"end":1380},"obj":"http://www.uniprot.org/uniprot/O15197"},{"id":"T9","span":{"begin":536,"end":539},"obj":"http://www.uniprot.org/uniprot/P08519"},{"id":"T10","span":{"begin":686,"end":688},"obj":"http://www.uniprot.org/uniprot/Q9NYU2"},{"id":"T11","span":{"begin":686,"end":688},"obj":"http://www.uniprot.org/uniprot/P51161"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":297,"end":299},"obj":"http://www.uniprot.org/uniprot/Q03404"},{"id":"T2","span":{"begin":686,"end":688},"obj":"http://www.uniprot.org/uniprot/P51162"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":220,"end":234},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/102234"},{"id":"T2","span":{"begin":220,"end":234},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1117"},{"id":"T3","span":{"begin":288,"end":299},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1167"},{"id":"T4","span":{"begin":288,"end":299},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1447071"},{"id":"T5","span":{"begin":349,"end":355},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/62951"},{"id":"T6","span":{"begin":445,"end":451},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/62951"},{"id":"T7","span":{"begin":1288,"end":1296},"obj":"http://purl.bioontology.org/ontology/STY/T033"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":112,"end":139},"obj":"http://purl.obolibrary.org/obo/GO_0000271"},{"id":"T2","span":{"begin":127,"end":139},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T3","span":{"begin":1381,"end":1393},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T4","span":{"begin":127,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0015943"},{"id":"T5","span":{"begin":141,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T6","span":{"begin":141,"end":168},"obj":"http://purl.obolibrary.org/obo/GO_0043158"},{"id":"T7","span":{"begin":235,"end":261},"obj":"http://purl.obolibrary.org/obo/GO_0043158"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":574,"end":578},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":809,"end":816},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":1231,"end":1238},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":574,"end":578},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T5","span":{"begin":809,"end":816},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T6","span":{"begin":1231,"end":1238},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T7","span":{"begin":574,"end":578},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T8","span":{"begin":809,"end":816},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T9","span":{"begin":1231,"end":1238},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T10","span":{"begin":574,"end":578},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T11","span":{"begin":809,"end":816},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12","span":{"begin":1231,"end":1238},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":104,"end":111},"obj":"http://purl.obolibrary.org/obo/GO_0009274"},{"id":"T2","span":{"begin":169,"end":177},"obj":"http://purl.obolibrary.org/obo/GO_0009274"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":220,"end":234},"obj":"http://purl.obolibrary.org/obo/MAT_0000192"}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G53038OI\""},{"id":"GlycanIUPAC_T2","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G53038OI\""},{"id":"GlycanIUPAC_T3","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G53038OI\""},{"id":"GlycanIUPAC_T4","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G53038OI\""},{"id":"GlycanIUPAC_T5","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G71412NI\""},{"id":"GlycanIUPAC_T6","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G71412NI\""},{"id":"GlycanIUPAC_T7","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G71412NI\""},{"id":"GlycanIUPAC_T8","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G71412NI\""},{"id":"GlycanIUPAC_T9","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G95181HA\""},{"id":"GlycanIUPAC_T10","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G95181HA\""},{"id":"GlycanIUPAC_T11","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G95181HA\""},{"id":"GlycanIUPAC_T12","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G95181HA\""},{"id":"GlycanIUPAC_T13","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G33888ZV\""},{"id":"GlycanIUPAC_T14","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G33888ZV\""},{"id":"GlycanIUPAC_T15","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G33888ZV\""},{"id":"GlycanIUPAC_T16","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G33888ZV\""},{"id":"GlycanIUPAC_T17","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G72383QV\""},{"id":"GlycanIUPAC_T18","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G72383QV\""},{"id":"GlycanIUPAC_T19","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G72383QV\""},{"id":"GlycanIUPAC_T20","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G72383QV\""},{"id":"GlycanIUPAC_T21","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G52595WA\""},{"id":"GlycanIUPAC_T22","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G52595WA\""},{"id":"GlycanIUPAC_T23","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G52595WA\""},{"id":"GlycanIUPAC_T24","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G52595WA\""},{"id":"GlycanIUPAC_T25","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G65441IM\""},{"id":"GlycanIUPAC_T26","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G65441IM\""},{"id":"GlycanIUPAC_T27","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G65441IM\""},{"id":"GlycanIUPAC_T28","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G65441IM\""},{"id":"GlycanIUPAC_T29","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G64989KP\""},{"id":"GlycanIUPAC_T30","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G64989KP\""},{"id":"GlycanIUPAC_T31","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G64989KP\""},{"id":"GlycanIUPAC_T32","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G64989KP\""},{"id":"GlycanIUPAC_T33","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G39900ZC\""},{"id":"GlycanIUPAC_T34","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G39900ZC\""},{"id":"GlycanIUPAC_T35","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G39900ZC\""},{"id":"GlycanIUPAC_T36","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G39900ZC\""},{"id":"GlycanIUPAC_T37","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G51147IJ\""},{"id":"GlycanIUPAC_T38","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G51147IJ\""},{"id":"GlycanIUPAC_T39","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G51147IJ\""},{"id":"GlycanIUPAC_T40","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G51147IJ\""},{"id":"GlycanIUPAC_T41","span":{"begin":194,"end":197},"obj":"\"http://rdf.glycoinfo.org/glycan/G42761PO\""},{"id":"GlycanIUPAC_T42","span":{"begin":281,"end":284},"obj":"\"http://rdf.glycoinfo.org/glycan/G42761PO\""},{"id":"GlycanIUPAC_T43","span":{"begin":356,"end":359},"obj":"\"http://rdf.glycoinfo.org/glycan/G42761PO\""},{"id":"GlycanIUPAC_T44","span":{"begin":1377,"end":1380},"obj":"\"http://rdf.glycoinfo.org/glycan/G42761PO\""},{"id":"GlycanIUPAC_T45","span":{"begin":937,"end":942},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T46","span":{"begin":1040,"end":1045},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T47","span":{"begin":937,"end":942},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T48","span":{"begin":1040,"end":1045},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T49","span":{"begin":937,"end":942},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""},{"id":"GlycanIUPAC_T50","span":{"begin":1040,"end":1045},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""}],"text":"Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.\nFormation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP\u0026glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate β/α/β Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes \"open-closed-open\" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway."}