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Biosynthesis of a conserved glycolipid anchor for Gram-negative bacterial capsules

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Title: Biosynthesis of a conserved glycolipid anchor for Gram-negative bacterial capsules
Author: Doyle, Liam; Ovchinnikova, Olga; Myler, Katherine; Mallette, Evan; Huang, Bo-Shun; Lowary, Todd; Kimber, Matthew; Whitfield, Chris
Department: Department of Molecular and Cellular Biology
Abstract: Several important Gram-negative bacterial pathogens possess surface capsular layers composed of hypervariable long-chain polysaccharides linked via a conserved β-Kdo oligosaccharide to a phosphatidylglycerol residue. The pathway for synthesis of the terminal glycolipid was elucidated by determining structures of reaction intermediates. In Escherichia coli, KpsS transfers a single Kdo residue to phosphatidylglycerol; this primer is extended using a single enzyme (KpsC), possessing two CMP-Kdo-dependent glycosyltransferase catalytic centres with different linkage specificities. The structure of the N-terminal β-(2→4)-Kdo transferase from KpsC reveals two α/β domains, supplemented by several additional helices. The N-terminal Rossmann-like domain, typically responsible for acceptor binding, is severely reduced in size compared to canonical GT-B folds in glycosyltransferases. The similar structure of the C-terminal β-(2→7)-Kdo transferase indicates a past gene duplication event. Both Kdo transferases have a narrow active site tunnel, lined with key residues shared with GT99 β-Kdo transferases. This enzyme provides the prototype for the GT107 family.
URI: https://hdl.handle.net/10214/26834
Date: 2019
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Related Publications: Doyle, L., Ovchinnikova, O.G., Myler, K., Mallette, E., Huang, B.-S., Lowary, T.L., Kimber, M.S., and Whitfield, C. (2019). Biosynthesis of a conserved glycolipid anchor for Gram-negative bacterial capsules. Nature Chemical Biology 15:632-640 doi: 10.1038/s41589-019-0276-8


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