1nq6
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(New page: 200px<br /><applet load="1nq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nq6, resolution 1.78Å" /> '''Crystal Structure of...)
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Revision as of 21:26, 24 November 2007
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Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8
Overview
Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They, are of increasing interest in the paper and food industries for their, pre-bleaching and bio-pulping applications. Such industries demand new, xylanases to cover a wider range of cleavage specificity, activity and, stability. The catalytic domain of xylanase Xys1 from Streptomyces, halstedii JM8 was expressed, purified and crystallized and native data, were collected to 1.78 A resolution with an R(merge) of 4.4%. The crystals, belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 A. The structure was solved by the, molecular-replacement method using the structure of the homologue Xyl10A, from Streptomyces lividans. In a similar manner to other members of its, family, Xys1 folds to form a standard (beta/alpha)(8) barrel with the two, catalytic functions, the acid/base and the nucleophile, at its C-terminal, side. The overall structure is described and compared with those of, related xylanases.
About this Structure
1NQ6 is a Single protein structure of sequence from Streptomyces halstedii with MG as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
Structure of xylanase Xys1delta from Streptomyces halstedii., Canals A, Vega MC, Gomis-Ruth FX, Diaz M, Santamaria R RI, Coll M, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1447-53. Epub 2003, Jul 23. PMID:12876348
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