6mgb

Publication Abstract from PubMed

Several important Gram-negative bacterial pathogens possess surface capsular layers composed of hypervariable long-chain polysaccharides linked via a conserved 3-deoxy-beta-D-manno-oct-2-ulosonic acid (beta-Kdo) oligosaccharide to a phosphatidylglycerol residue. The pathway for synthesis of the terminal glycolipid was elucidated by determining the 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 cytidine 5'-monophosphate (CMP)-Kdo-dependent glycosyltransferase catalytic centers with different linkage specificities. The structure of the N-terminal beta-(2-->4) Kdo transferase from KpsC reveals two alpha/beta domains, supplemented by several helices. The N-terminal Rossmann-like domain, typically responsible for acceptor binding, is severely reduced in size compared with canonical GT-B folds in glycosyltransferases. The similar structure of the C-terminal beta-(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 beta-Kdo transferases. This enzyme provides the prototype for the GT107 family.

Biosynthesis of a conserved glycolipid anchor for Gram-negative bacterial capsules.,Doyle L, Ovchinnikova OG, Myler K, Mallette E, Huang BS, Lowary TL, Kimber MS, Whitfield C Nat Chem Biol. 2019 Jun;15(6):632-640. doi: 10.1038/s41589-019-0276-8. Epub 2019 , Apr 29. PMID:31036922^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.