Journal Article

PUBDB-2016-00529

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide

Hagelueken, G. ; Clarke, B. R. ; Huang, H. ; Tuukkanen, A. ; Danciu, I. ; Svergun, D.EMBL* ; Hussain, R. ; Liu, H. ; Whitfield, C. (Corresponding author) ; Naismith, J. H. (Corresponding author)

2014
Nature Publishing Group London [u.a.]

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Please use a persistent id in citations: doi:10.1038/nsmb.2935

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.

Note: (c) Macmillan Publishers Limited. Post referee full text in progress.

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Contributing Institute(s):

1. EMBL (EMBL)
2. EMBL-User (EMBL-User)

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Experiment(s):

1. Facility (machine) DORIS III

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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