3GTN
Crystal Structure of XynC from Bacillus subtilis 168
Summary for 3GTN
Entry DOI | 10.2210/pdb3gtn/pdb |
Descriptor | Glucuronoxylanase xynC (1 entity in total) |
Functional Keywords | xylanase, glycosyl hydrolase family 5, gh5, gh 5, xync, bacillus subtilis, glucuronoxylan, glycosyl hydrolase, carbohydrate metabolism, glycosidase, hydrolase, polysaccharide degradation, secreted, xylan degradation |
Biological source | Bacillus subtilis |
Cellular location | Secreted : Q45070 |
Total number of polymer chains | 2 |
Total formula weight | 90862.93 |
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 citation | St 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: 19407387DOI: 10.1107/S1744309109013098 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.68 Å) |
Structure validation
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