Structure of WbdD: a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in Escherichia coli O9a

• Published in: Molecular microbiology Vol. 86; no. 3; pp. 730 - 742
• Main Authors: Hagelueken, Gregor, Huang, Hexian, Clarke, Bradley R., Lebl, Tomas, Whitfield, Chris, Naismith, James H.
• Format: Journal Article
• Language: English
• Published: England Blackwell Publishing Ltd 01.11.2012
• Subjects: Amino Acid Sequence; Antigens; Biosynthesis; Carbohydrates; E coli; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - enzymology; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Eukaryotes; Kinases; Methyltransferases - chemistry; Methyltransferases - genetics; Methyltransferases - metabolism; Models, Molecular; Molecular Sequence Data; Mutagenesis; O Antigens - chemistry; O Antigens - metabolism; Polysaccharides, Bacterial - chemistry; Polysaccharides, Bacterial - metabolism; Protein Kinases - chemistry; Protein Kinases - genetics; Protein Kinases - metabolism; Protein Structure, Tertiary; Sequence Alignment; Substrate Specificity

Summary The 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. The polymannose O9a O‐PS is synthesized as a polyprenol‐linked glycan by mannosyltransferase enzymes located at the cytop...