Home > Publications database > A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide > print |
001 | 293440 | ||
005 | 20210709143651.0 | ||
024 | 7 | _ | |a 10.1038/nsmb.2935 |2 doi |
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100 | 1 | _ | |a Hagelueken, Gregor |b 0 |
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 |
336 | 7 | _ | |a article |2 DRIVER |
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336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1470228481_29732 |2 PUB:(DE-HGF) |
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500 | _ | _ | |a (c) Macmillan Publishers Limited. Post referee full text in progress. |
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 |b 1 |
700 | 1 | _ | |a Huang, Hexian |b 2 |
700 | 1 | _ | |a Tuukkanen, Anne |b 3 |
700 | 1 | _ | |a Danciu, Iulia |b 4 |
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700 | 1 | _ | |a Hussain, Rohanah |0 P:(DE-HGF)0 |b 6 |
700 | 1 | _ | |a Liu, Huanting |b 7 |
700 | 1 | _ | |a Whitfield, Chris |0 P:(DE-HGF)0 |b 8 |e Corresponding author |
700 | 1 | _ | |a Naismith, James H |0 P:(DE-HGF)0 |b 9 |e Corresponding author |
773 | _ | _ | |a 10.1038/nsmb.2935 |g Vol. 22, no. 1, p. 50 - 56 |0 PERI:(DE-600)2131437-8 |n 1 |p 50 - 56 |t Nature structural & molecular biology |v 22 |y 2014 |x 1545-9985 |
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910 | 1 | _ | |a Europäisches Laboratorium für Molekularbiologie |0 I:(DE-588b)235011-7 |k EMBL |b 5 |6 P:(DE-H253)PIP1001422 |
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