PubMed:8063693 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":131},"obj":"Sentence"},{"id":"T2","span":{"begin":132,"end":378},"obj":"Sentence"},{"id":"T3","span":{"begin":379,"end":490},"obj":"Sentence"},{"id":"T4","span":{"begin":491,"end":562},"obj":"Sentence"},{"id":"T5","span":{"begin":563,"end":579},"obj":"Sentence"},{"id":"T6","span":{"begin":580,"end":592},"obj":"Sentence"},{"id":"T7","span":{"begin":593,"end":645},"obj":"Sentence"},{"id":"T8","span":{"begin":646,"end":876},"obj":"Sentence"},{"id":"T9","span":{"begin":877,"end":943},"obj":"Sentence"},{"id":"T10","span":{"begin":944,"end":1146},"obj":"Sentence"},{"id":"T11","span":{"begin":1147,"end":1161},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":131},"obj":"Sentence"},{"id":"T2","span":{"begin":132,"end":378},"obj":"Sentence"},{"id":"T3","span":{"begin":379,"end":490},"obj":"Sentence"},{"id":"T4","span":{"begin":491,"end":562},"obj":"Sentence"},{"id":"T5","span":{"begin":563,"end":579},"obj":"Sentence"},{"id":"T6","span":{"begin":580,"end":592},"obj":"Sentence"},{"id":"T7","span":{"begin":593,"end":645},"obj":"Sentence"},{"id":"T8","span":{"begin":646,"end":876},"obj":"Sentence"},{"id":"T9","span":{"begin":877,"end":943},"obj":"Sentence"},{"id":"T10","span":{"begin":944,"end":1146},"obj":"Sentence"},{"id":"T11","span":{"begin":1147,"end":1161},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases.\nThe crystal structure of the 32-kDa catalytic domain of the Streptomyces lividans xylanase A was solved by molecular isomorphous replacement methods and subsequently refined at 2.6-A resolution to a conventional crystallographic R factor of 0.21. This is the first successful structure determination of a member of the F family of endo-beta-1,4-D-glycanases. Unlike the recently determined xylanases of the G family (Wakarchuk, W. W., Campbell, R. L., Sung, W. L., Davoodi, J., and Yaguchi, M. (1994) Protein Sci. 3, 467-475), where the catalytic domains have a unique beta-sheet structure, the 32-kDa domain of the S. lividans xylanase A is folded into a complete (alpha/beta)8 barrel, the first such fold observed among beta-1,4-D-glycanases. The active site is located at the carbonyl end of the beta barrel. The crystal structure supports the earlier assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R. (1994) Biochem. J., in press)."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":47,"end":68},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":192,"end":213},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1051,"end":1060},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1916"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1916"},{"id":"A3","pred":"db_id","subj":"T3","obj":"404338"}],"text":"Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases.\nThe crystal structure of the 32-kDa catalytic domain of the Streptomyces lividans xylanase A was solved by molecular isomorphous replacement methods and subsequently refined at 2.6-A resolution to a conventional crystallographic R factor of 0.21. This is the first successful structure determination of a member of the F family of endo-beta-1,4-D-glycanases. Unlike the recently determined xylanases of the G family (Wakarchuk, W. W., Campbell, R. L., Sung, W. L., Davoodi, J., and Yaguchi, M. (1994) Protein Sci. 3, 467-475), where the catalytic domains have a unique beta-sheet structure, the 32-kDa domain of the S. lividans xylanase A is folded into a complete (alpha/beta)8 barrel, the first such fold observed among beta-1,4-D-glycanases. The active site is located at the carbonyl end of the beta barrel. The crystal structure supports the earlier assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R. (1994) Biochem. J., in press)."}