1xas
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(New page: 200px<br /><applet load="1xas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xas, resolution 2.6Å" /> '''CRYSTAL STRUCTURE, AT...)
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Revision as of 03:49, 21 November 2007
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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
Overview
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).
About this Structure
1XAS is a Single protein structure of sequence from Streptomyces lividans. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
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., Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS, J Biol Chem. 1994 Aug 19;269(33):20811-4. PMID:8063693
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