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From Proteopedia

Revision as of 13:47, 30 October 2007

CRYSTAL STRUCTURE OF CHONDROITINASE B COMPLEXED TO DERMATAN SULFATE HEXASACCHARIDE

Overview

Chondroitinase B from Pedobacter heparinus is the only known enzyme, strictly specific for dermatan sulfate and is a widely used enzymatic tool, for the structural characterization of glycosaminoglycans. This, beta-helical polysaccharide lyase belongs to family PL-6 and cleaves the, beta(1,4) linkage of dermatan sulfate in a random manner, yielding, 4,5-unsaturated dermatan sulfate disaccharides as the product. The, previously reported structure of its complex with a dermatan sulfate, disaccharide product identified the -1 and -2 subsites of the catalytic, groove. We present here the structure of chondroitinase B complexed with, several dermatan sulfate and chondroitin sulfate oligosaccharides. In, particular, the soaking of chondroitinase B crystals with a dermatan, sulfate ... [(full description)]

About this Structure

1OFL is a [Single protein] structure of sequence from [Pedobacter heparinus] with GLA, BGC, CA and MXZ as [ligands]. Active as [Transferred entry: 4.2.2.20], with EC number [4.2.2.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic machinery., Michel G, Pojasek K, Li Y, Sulea T, Linhardt RJ, Raman R, Prabhakar V, Sasisekharan R, Cygler M, J Biol Chem. 2004 Jul 30;279(31):32882-96. Epub 2004 May 21. PMID:15155751

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