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| '''CRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSES'''
| | ===CRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSES=== |
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| ==Overview==
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| The 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). | | The line below this paragraph, {{ABSTRACT_PUBMED_8063693}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8063693 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8063693}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Derewenda, Z S.]] | | [[Category: Derewenda, Z S.]] |
| [[Category: Xylanase some]] | | [[Category: Xylanase some]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:47:34 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:19:41 2008'' |