%0 Journal Article
%A Hagelueken, Gregor
%A Clarke, Bradley R
%A Huang, Hexian
%A Tuukkanen, Anne
%A Danciu, Iulia
%A Svergun, Dmitri
%A Hussain, Rohanah
%A Liu, Huanting
%A Whitfield, Chris
%A Naismith, James H
%T A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide
%J Nature structural & molecular biology
%V 22
%N 1
%@ 1545-9985
%C London [u.a.]
%I Nature Publishing Group
%M PUBDB-2016-00529
%P 50 - 56
%D 2014
%Z (c) Macmillan Publishers Limited. Post referee full text in progress.
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000347664700010
%$ pmid:25504321
%R 10.1038/nsmb.2935
%U https://bib-pubdb1.desy.de/record/293440