1ro7
From Proteopedia
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Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.
Overview
Sialic acid terminates oligosaccharide chains on mammalian and microbial, cell surfaces, playing critical roles in recognition and adherence. The, enzymes that transfer the sialic acid moiety from, cytidine-5'-monophospho-N-acetyl-neuraminic acid (CMP-NeuAc) to the, terminal positions of these key glycoconjugates are known as, sialyltransferases. Despite their important biological roles, little is, understood about the mechanism or molecular structure of these, membrane-associated enzymes. We report the first structure of a, sialyltransferase, that of CstII from Campylobacter jejuni, a highly, prevalent foodborne pathogen. Our structural, mutagenesis and kinetic data, provide support for a novel mode of substrate binding and glycosyl, transfer mechanism, including essential roles of a histidine (general, base) and two tyrosine residues (coordination of the phosphate leaving, group). This work provides a framework for understanding the activity of, several sialyltransferases, from bacterial to human, and for the, structure-based design of specific inhibitors.
About this Structure
1RO7 is a Single protein structure of sequence from Campylobacter jejuni with CSF and MPD as ligands. Full crystallographic information is available from OCA.
Reference
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog., Chiu CP, Watts AG, Lairson LL, Gilbert M, Lim D, Wakarchuk WW, Withers SG, Strynadka NC, Nat Struct Mol Biol. 2004 Feb;11(2):163-70. Epub 2004 Jan 18. PMID:14730352
Page seeded by OCA on Sat Nov 24 23:00:55 2007
