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- Title
A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide.
- Authors
Hagelueken, Gregor; Clarke, Bradley R; Huang, Hexian; Tuukkanen, Anne; Danciu, Iulia; Svergun, Dmitri I; Hussain, Rohanah; Liu, Huanting; Whitfield, Chris; Naismith, James H
- Abstract
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.
- Subjects
LIPOPOLYSACCHARIDES; ESCHERICHIA coli; ENDOTOXINS; ESCHERICHIA; O antigens
- Publication
Nature Structural & Molecular Biology, 2015, Vol 22, Issue 1, p50
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2935