3GTN

Crystal Structure of XynC from Bacillus subtilis 168

3GTN の概要

• エントリーDOI: 10.2210/pdb3gtn/pdb
• 分子名称: Glucuronoxylanase xynC (1 entity in total)
• 機能のキーワード: xylanase, glycosyl hydrolase family 5, gh5, gh 5, xync, bacillus subtilis, glucuronoxylan, glycosyl hydrolase, carbohydrate metabolism, glycosidase, hydrolase, polysaccharide degradation, secreted, xylan degradation
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Secreted : Q45070
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90862.93

構造登録者

St John, F.J.,Hurlbert, J.C.,Pozharski, E. (登録日: 2009-03-27, 公開日: 2009-04-28, 最終更新日: 2024-02-21)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.68 Å)