1ofm
From Proteopedia
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CRYSTAL STRUCTURE OF CHONDROITINASE B COMPLEXED TO CHONDROITIN 4-SULFATE TETRASACCHARIDE
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
1OFM is a [Single protein] structure of sequence from [Pedobacter heparinus] with GLA, BGC and MXZ as [ligands]. Active as [[1]], with EC number [4.2.2.4]. 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
Page seeded by OCA on Mon Oct 29 19:52:12 2007
Categories: Pedobacter heparinus | Single protein | Cygler, M. | Michel, G. | BGC | GLA | MXZ | Active site | Beta-elimination | Chondroitin 4-sulfate | Lyase
