Open AccessCrystallization and crystallographic analysis of Bacillus subtilis xylanase C
Author(s) -
St John Franz J.,
Godwin David K.,
Preston James F.,
Pozharski Edwin,
Hurlbert Jason C.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109013098
Subject(s) - xylanase , bacillus subtilis , glycosyl , chemistry , glycoside hydrolase , hydrolase , crystallization , monoclinic crystal system , biochemistry , moiety , depolymerization , resolution (logic) , crystallography , stereochemistry , enzyme , biology , crystal structure , bacteria , genetics , organic chemistry , artificial intelligence , computer science
The recent biochemical characterization of the xylanases of glycosyl hydrolase family 5 (GH 5) has identified a distinctive endo mode of action, hydrolyzing the β‐1,4 xylan chain at a specific site directed by the position of an α‐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 Å resolution density map. The crystals belonged to the primitive monoclinic space group P 2 1 . Further screening identified an additive that resulted in large reproducible crystals. This larger more robust crystal form belonged to space group P 2 1 2 1 2 and a resulting data set has been processed to 1.64 Å 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.