1v7x | pdb_00001v7x
Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc and sulfate
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Overview
Vibrio proteolyticus chitobiose phosphorylase (ChBP) belongs to glycosyl, transferase family 36 (GT-36), and catalyzes the reversible phosphorolysis, of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of, the anomeric configuration. As the first known structures of a GT-36, enzyme, we determined the crystal structure of ChBP in a ternary complex, with GlcNAc and SO(4). It is also the first structures of an inverting, phosphorolytic enzyme in a complex with a sugar and a sulfate ion, and, reveals a pseudo-ternary complex structure of enzyme-sugar-phosphate. ChBP, comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain, constituting a distinctive structure among GT families. Instead, it shows, significant structural similarity with glycoside hydrolase (GH) enzymes, glucoamylases (GH-15), and maltose phosphorylase (GH-65) in clan GH-L. The, structural similarity reported here, together with distant sequence, similarities between ChBP and GHs, led to the reclassification of family, GT-36 into a novel GH family, namely GH-94.
About this Structure
1V7X is a Single protein structure of sequence from Vibrio proteolyticus with NDG, NAG, CA and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (alpha/alpha)(6) barrel fold., Hidaka M, Honda Y, Kitaoka M, Nirasawa S, Hayashi K, Wakagi T, Shoun H, Fushinobu S, Structure. 2004 Jun;12(6):937-47. PMID:15274915
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