3gtn

Crystal Structure of XynC from Bacillus subtilis 168

spinqualitylabelsall models 3gtn, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gtn is a 2 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: BSU18150, xynC, ynfF ("Vibrio subtilis" Ehrenberg 1835) Activity: Glucuronoarabinoxylan endo-1,4-beta-xylanase, with EC number 3.2.1.136 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [XYNC_BACSU] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA). 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 The recent biochemical characterization of the xylanases of glycosyl hydrolase family 5 (GH 5) has identified a distinctive endo mode of action, hydrolyzing the beta-1,4 xylan chain at a specific site directed by the position of an alpha-1,2-linked glucuronate moiety. Xylanase C (XynC), the GH 5 xylanase from Bacillus subtilis 168, has been cloned, overexpressed and crystallized. Initial data collection was performed and a preliminary model has been built into a low-quality 2.7 A resolution density map. The crystals belonged to the primitive monoclinic space group P2(1). Further screening identified an additive that resulted in large reproducible crystals. This larger more robust crystal form belonged to space group P2(1)2(1)2 and a resulting data set has been processed to 1.64 A resolution. This will be the second structure to be solved from this unique xylanase family and the first from a Gram-positive bacterium. This work may help to identify the structural determinants that allow the exceptional specificity of this enzyme and the role it plays in the biological depolymerization and processing of glucuronoxylan. Crystallization and crystallographic analysis of Bacillus subtilis xylanase C.,St John FJ, Godwin DK, Preston JF, Pozharski E, Hurlbert JC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):499-503. Epub 2009 Apr 24. PMID:19407387 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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