1h5v

From Proteopedia

Revision as of 13:25, 30 October 2007

THIOPENTASACCHARIDE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHARENS AT 1.1 A RESOLUTION IN THE TETRAGONAL CRYSTAL FORM

Overview

Many three-dimensional structures of retaining beta-D-glycoside hydrolases, have been determined, yet oligosaccharide complexes in which the ligand, spans the catalytic centre are rare. Those that have been reported so far, have revealed two modes of binding: those in which the substrate adopts a, distorted skew-boat or envelope conformation in the -1 subsite, reflecting, the distortion observed during the catalytic cycle, and those which bypass, the true catalytic centre and thus lie in a non-productive manner across, the -1 subsite. The three-dimensional structure of a retaining, endocellulase, Bacillus agaradhaerens Cel5A, in complex with methyl, 4,4(II),4(III),4(IV)-tetrathio-alpha-cellopentoside falls into this latter, category. The 1.1 A structure reveals the binding of five ... [(full description)]

About this Structure

1H5V is a [Single protein] structure of sequence from [Bacillus agaradhaerens] with GLC, SSG, SGC, MA3, CA and NA as [ligands]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: ACI. Full crystallographic information is available from [OCA].

Reference

Atomic resolution structure of endoglucanase Cel5A in complex with methyl 4,4II,4III,4IV-tetrathio-alpha-cellopentoside highlights the alternative binding modes targeted by substrate mimics., Varrot A, Schulein M, Fruchard S, Driguez H, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1739-42. Epub 2001, Oct 25. PMID:11679762

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