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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.

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488 nm laseruses

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Norland Electrical Adhesives · Dispensers ... Norland Optical Adhesive 142 is a clear liquid ... product. Prolonged contact with skin should be ...

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7 days ago — like I've taught you. with the tinctures. That's also very powerful. for cleaning out a UTI infection. Just a simple. basic clove shot. Put some ...

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We thank the US Department of Energy for access to data collection facilities at the NSLS, and also M. Karwaski and S. Ryan for technical help. We thank Neose Pharmaceuticals for providing sialyllactose and CMP-NeuAc for the kinetic studies. The work was funded by the Howard Hughes Medical Institute, the Canadian Institute of Health Research and the Burroughs Wellcome Foundation (to N.S.), the Natural Sciences and Engineering Research Council and a Human Frontiers Science Grant (to S.W.) and by the National Research Council–GH (to W.W. and M.G.).

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