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3GTN

Crystal Structure of XynC from Bacillus subtilis 168

Summary for 3GTN
Entry DOI10.2210/pdb3gtn/pdb
DescriptorGlucuronoxylanase xynC (1 entity in total)
Functional Keywordsxylanase, glycosyl hydrolase family 5, gh5, gh 5, xync, bacillus subtilis, glucuronoxylan, glycosyl hydrolase, carbohydrate metabolism, glycosidase, hydrolase, polysaccharide degradation, secreted, xylan degradation
Biological sourceBacillus subtilis
Cellular locationSecreted : Q45070
Total number of polymer chains2
Total formula weight90862.93
Authors
St John, F.J.,Hurlbert, J.C.,Pozharski, E. (deposition date: 2009-03-27, release date: 2009-04-28, Last modification date: 2024-02-21)
Primary citationSt John, F.J.,Godwin, D.K.,Preston, J.F.,Pozharski, E.,Hurlbert, J.C.
Crystallization and crystallographic analysis of Bacillus subtilis xylanase C.
Acta Crystallogr.,Sect.F, 65:499-503, 2009
Cited by
PubMed Abstract: 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.
PubMed: 19407387
DOI: 10.1107/S1744309109013098
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.68 Å)
Structure validation

231029

數據於2025-02-05公開中

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