1ro7: Difference between revisions

[[Image:1ro7.gif|left|200px]]<br /><applet load="1ro7" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

1RO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] with <scene name='pdbligand=CSF:'>CSF</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO7 OCA].  

[[Category: Chiu, C P.]]

[[Category: Lairson, L L.]]

[[Category: Strynadka, N C.]]

[[Category: Wakarchuk, W W.]]

[[Category: Watts, A G.]]

[[Category: Withers, S G.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:52 2008''