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Structure of WbdD; a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in Escherichia coliO9a

DOI: 10.1111/mmi.12014 DOI Help
PMID: 22970759 PMID Help

Authors: Gregor Hagelueken (University of St Andrews) , Hexian Huang (University of St Andrews) , Bradley R. Clarke (University of Guelph) , Thomas Lebl (University of St Andrews) , Chris Whitfield (University of Guelph) , James H. Naismith (University of St Andrews)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Microbiology

State: Published (Approved)
Published: September 2012
Diamond Proposal Number(s): 7705

Abstract: Escherichia coli serotype O9a O-antigen polysaccharide (O-PS) is a model for glycan biosynthesis and export by the ATP-binding cassette transporter-dependent pathway, polyprenol-linked glycan by mannosyltransferase enzymes, cytoplasmic membrane,WbdD first phosphorylates the terminal non-reducing mannose of the O-PS and then methylates the phosphate, stopping polymerization, The kinase domain is again fused to an extended C-terminal coiled-coil domain reminiscent of eukaryotic DMPK (Myotonic Dystrophy Protein Kinase) family kinases such as Rho-associated protein kinase (ROCK). WbdD phosphorylates 2-á-d-mannosyl-d-mannose (2á-MB), a short mimic of the O9a polymer, protein kinase inhibitors

Journal Keywords: Escherichia; Methyltransferases; Models; Molecular; O; Polysaccharides; Bacterial; Protein; Tertiary; Sequence; Substrate Specificity

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 24/09/2012 11:01

Molecular Microbiology - 2012 - Hagelueken - Structure of WbdD a bifunctional kinase and methyltransferase that regulates.pdf

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)