Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
