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1ro7

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[[Image:1ro7.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1ro7", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CSF:CYTIDINE-5&#39;-MONOPHOSPHATE-3-FLUORO-N-ACETYL-NEURAMINIC+ACID'>CSF</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|GENE= cst ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 Campylobacter jejuni])
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{{STRUCTURE_1ro7| PDB=1ro7 | SCENE= }}
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|RELATEDENTRY=[[1ro8|1RO8]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ro7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ro7 OCA], [http://www.ebi.ac.uk/pdbsum/1ro7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ro7 RCSB]</span>
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'''Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.'''
'''Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.'''
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[[Category: Watts, A G.]]
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[[Category: Withers, S G.]]
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[[Category: mixed alpha/beta]]
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[[Category: Mixed alpha/beta]]
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[[Category: rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:43:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:30:47 2008''
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Revision as of 04:43, 3 May 2008

Template:STRUCTURE 1ro7

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. 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 May 3 07:43:20 2008

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