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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
PMID:
22970759
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
Discipline Tags:
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)