TY  - JOUR
AU  - Hagelueken, Gregor
AU  - Clarke, Bradley R
AU  - Huang, Hexian
AU  - Tuukkanen, Anne
AU  - Danciu, Iulia
AU  - Svergun, Dmitri
AU  - Hussain, Rohanah
AU  - Liu, Huanting
AU  - Whitfield, Chris
AU  - Naismith, James H
TI  - A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide
JO  - Nature structural & molecular biology
VL  - 22
IS  - 1
SN  - 1545-9985
CY  - London [u.a.]
PB  - Nature Publishing Group
M1  - PUBDB-2016-00529
SP  - 50 - 56
PY  - 2014
N1  - (c) Macmillan Publishers Limited. Post referee full text in progress.
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000347664700010
C6  - pmid:25504321
DO  - DOI:10.1038/nsmb.2935
UR  - https://bib-pubdb1.desy.de/record/293440
ER  -