1h1a

From Proteopedia

Revision as of 13:20, 30 October 2007

THERMOPHILIC B-1,4-XYLANASE FROM CHAETOMIUM THERMOPHILUM

Overview

The crystal structures of thermophilic xylanases from Chaetomium, thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A, resolution, respectively. Both enzymes have the overall fold typical to, family 11 xylanases with two highly twisted beta-sheets forming a large, cleft. The comparison of 12 crystal structures of family 11 xylanases from, both mesophilic and thermophilic organisms showed that the structures of, different xylanases are very similar. The sequence identity differences, correlated well with the structural differences. Several minor, modifications appeared to be responsible for the increased thermal, stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased, number of charged residues, especially Arg, resulting in enhanced polar, ... [(full description)]

About this Structure

1H1A is a [Single protein] structure of sequence from [Chaetomium thermophilum] with SO4, CA, S and GOL as [ligands]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: S1A. Full crystallographic information is available from [OCA].

Reference

Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability., Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J, Eur J Biochem. 2003 Apr;270(7):1399-412. PMID:12653995

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