1nq6

Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8

spinqualitylabelsall models 1nq6, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nq6 is a 1 chain structure with sequence from Streptomyces halstedii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q59922_STRHA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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