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 separates WbdA from the catalytic domain of WbdD. The effects of insertions and deletions in the coiled-coil region were analyzed in vivo, revealing that polymer size is controlled by varying the length of the coiled-coil domain. Thus, the coiled-coil domain of WbdD functions as a molecular ruler that, along with WbdA:WbdD stoichiometry, controls the chain length of a model bacterial polysaccharide.
A coiled-coil domain acts as a molecular ruler in LPS chain length regulation
G. Hagelueken,B. Clarke,Hexian Huang,A. Tuukkanen,Iulia Danciu,D. Svergun,R. Hussain,Huanting Liu,C. Whitfield,J. Naismith
Published 2014 in Nature Structural &Molecular Biology
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- Publication year
2014
- Venue
Nature Structural &Molecular Biology
- Publication date
2014-11-25
- Fields of study
Biology, Medicine, Chemistry
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Semantic Scholar, PubMed
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