2fuz
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(New page: 200px<br /><applet load="2fuz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fuz, resolution 1.80Å" /> '''UGL hexagonal crysta...)
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Revision as of 08:39, 21 November 2007
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UGL hexagonal crystal structure without glycine and DTT molecules
Overview
Bacterial unsaturated glucuronyl hydrolases (UGLs) together with, polysaccharide lyases are responsible for the complete depolymerization of, mammalian extracellular matrix glycosaminoglycans. UGL acts on various, oligosaccharides containing unsaturated glucuronic acid (DeltaGlcA) at the, nonreducing terminus and releases DeltaGlcA through hydrolysis. In this, study, we demonstrate the substrate recognition mechanism of the UGL of, Bacillus sp. GL1 by determining the X-ray crystallographic structure of, its substrate-enzyme complexes. The tetrasaccharide-enzyme complex, demonstrated that at least four subsites are present in the active pocket., Although several amino acid residues are crucial for substrate binding, the enzyme strongly recognizes DeltaGlcA at subsite -1 through the, formation of hydrogen bonds and stacking interactions, and prefers, N-acetyl-d-galactosamine and glucose rather than N-acetyl-d-glucosamine as, a residue accommodated in subsite +1, due to the steric hindrance.
About this Structure
2FUZ is a Single protein structure of sequence from Bacillus sp. with MPD as ligand. Full crystallographic information is available from OCA.
Reference
Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1., Itoh T, Hashimoto W, Mikami B, Murata K, Biochem Biophys Res Commun. 2006 May 26;344(1):253-62. PMID:16630576
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