A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide.
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ABSTRACT:
SUBMITTER: Hagelueken G
PROVIDER: S-EPMC4650267 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Publications
A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide.
Hagelueken Gregor G Clarke Bradley R BR Huang Hexian H Tuukkanen Anne A Danciu Iulia I Svergun Dmitri I DI Hussain Rohanah R Liu Huanting H Whitfield Chris C Naismith James H JH
Nature structural & molecular biology 20141215 1
Long-chain bacterial polysaccharides have important roles in pathogenicity. In Escherichia coli O9a, a model for ABC transporter-dependent polysaccharide assembly, a large extracellular carbohydrate with a narrow size distribution is polymerized from monosaccharides by a complex of two proteins, WbdA (polymerase) and WbdD (terminating protein). Combining crystallography and small-angle X-ray scattering, we found that the C-terminal domain of WbdD contains an extended coiled-coil that physically ...[more]
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