| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-140 |
Sentence |
denotes |
Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis. |
| T1 |
0-140 |
Sentence |
denotes |
Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis. |
| T1 |
0-140 |
Sentence |
denotes |
Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis. |
| TextSentencer_T2 |
141-262 |
Sentence |
denotes |
Formation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. |
| T2 |
141-262 |
Sentence |
denotes |
Formation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. |
| T2 |
141-262 |
Sentence |
denotes |
Formation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. |
| TextSentencer_T3 |
263-482 |
Sentence |
denotes |
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. |
| T3 |
263-482 |
Sentence |
denotes |
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. |
| T3 |
263-482 |
Sentence |
denotes |
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. |
| TextSentencer_T4 |
483-636 |
Sentence |
denotes |
Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP&glucose and UDP, respectively. |
| T4 |
483-636 |
Sentence |
denotes |
Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP&glucose and UDP, respectively. |
| T4 |
483-636 |
Sentence |
denotes |
Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP&glucose and UDP, respectively. |
| TextSentencer_T5 |
637-825 |
Sentence |
denotes |
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. |
| T5 |
637-825 |
Sentence |
denotes |
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. |
| T5 |
637-825 |
Sentence |
denotes |
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. |
| TextSentencer_T6 |
826-949 |
Sentence |
denotes |
Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. |
| T6 |
826-949 |
Sentence |
denotes |
Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. |
| T6 |
826-949 |
Sentence |
denotes |
Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. |
| TextSentencer_T7 |
950-1074 |
Sentence |
denotes |
Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. |
| T7 |
950-1074 |
Sentence |
denotes |
Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. |
| T7 |
950-1074 |
Sentence |
denotes |
Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. |
| TextSentencer_T8 |
1075-1281 |
Sentence |
denotes |
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. |
| T8 |
1075-1281 |
Sentence |
denotes |
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. |
| T8 |
1075-1281 |
Sentence |
denotes |
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. |
| TextSentencer_T9 |
1282-1402 |
Sentence |
denotes |
These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway. |
| T9 |
1282-1402 |
Sentence |
denotes |
These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway. |
| T9 |
1282-1402 |
Sentence |
denotes |
These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway. |