2x61

Crystal structure of the sialyltransferase CST-II in complex with trisaccharide acceptor and CMP

spinqualitylabelsall models 2x61, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x61 is a 2 chain structure with sequence from Campylobacter jejuni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: ACT, CH, EDO, GAL, MPD, NGA, SIA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9LAK3_CAMJU Publication Abstract from PubMed Sialic acids play important roles in various biological processes and typically terminate the oligosaccharide chains on the cell surfaces of a wide range of organisms including mammals and bacteria. Their attachment is catalyzed by a set of sialyltransferases with defined specificities both for their acceptor sugars and the position of attachment. However, little is known of how this specificity is encoded. The structure of the bifunctional sialyltransferase Cst-II of the human pathogen Campylobacter jejuni in complex with CMP and the terminal trisaccharide of its natural acceptor (Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc) has been solved at 1.95 A resolution and its kinetic mechanism shown to be iso-ordered Bi Bi, consistent with its dual acceptor substrate specificity. The trisaccharide acceptor is seen to bind to the active site of Cst-II through interactions primarily mediated by Asn-51, Tyr-81, and Arg-129. Kinetic and structural analyses of mutants modified at these positions indicate that these residues are critical for acceptor binding and catalysis, thereby providing significant new insight into the kinetic and catalytic mechanism and acceptor specificity of this pathogen encoded bifunctional GT-42 sialyltransferase. Structural and kinetic analysis of substrate binding to the sialyltransferase CST-II from Campylobacter Jejuni.,Lee HJ, Lairson LL, Rich JR, Lameignere E, Wakarchuk WW, Withers SG, Strynadka NC J Biol Chem. 2011 Aug 8. PMID:21832050 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sialyltransferase Sialyltransferase 3D structures

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