1RO7

Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.

Summary for 1RO7

• Entry DOI: 10.2210/pdb1ro7/pdb
• Related: 1RO8
• Descriptor: alpha-2,3/8-sialyltransferase, (4S)-2-METHYL-2,4-PENTANEDIOL, CYTIDINE-5'-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC ACID, ... (4 entities in total)
• Functional Keywords: mixed alpha/beta, rossmann fold, transferase
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 4
• Total formula weight: 125569.46

Authors

Chiu, C.P.,Watts, A.G.,Lairson, L.L.,Gilbert, M.,Lim, D.,Wakarchuk, W.W.,Withers, S.G.,Strynadka, N.C. (deposition date: 2003-12-01, release date: 2004-02-03, Last modification date: 2024-10-09)

Primary citation

Chiu, C.P.,Watts, A.G.,Lairson, L.L.,Gilbert, M.,Lim, D.,Wakarchuk, W.W.,Withers, S.G.,Strynadka, N.C.
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog.
Nat.Struct.Mol.Biol., 11:163-170, 2004

PubMed Abstract: 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.

PubMed: 14730352
DOI: 10.1038/nsmb720

Experimental method

X-RAY DIFFRACTION (1.8 Å)