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100 1 _ |a Hagelueken, Gregor
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245 _ _ |a A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide
260 _ _ |a London [u.a.]
|c 2014
|b Nature Publishing Group
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520 _ _ |a 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.
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700 1 _ |a Clarke, Bradley R
|0 0000-0003-2233-1268
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700 1 _ |a Huang, Hexian
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700 1 _ |a Tuukkanen, Anne
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700 1 _ |a Danciu, Iulia
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700 1 _ |a Svergun, Dmitri
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700 1 _ |a Hussain, Rohanah
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700 1 _ |a Liu, Huanting
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700 1 _ |a Whitfield, Chris
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700 1 _ |a Naismith, James H
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773 _ _ |a 10.1038/nsmb.2935
|g Vol. 22, no. 1, p. 50 - 56
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