Fadouloglou, V.E., Tampakaki, A.P., Glykos, N.M., Bastaki, M.N, Hadden, J.M., Phillips, S.E.V., Panopoulos, N.J. and Kokkinidis, M. (2004) Structure of HrcQ(B)-C, a conserved component of the bacterial type III secretion systems. Proceedings of the National Academy of Sciences, 101 (1). pp. 70-75. ISSN 0027-8424Full text available as:
Available under licence : See the attached licence file.
Type III secretion systems enable plant and animal bacterial pathogens to deliver virulence proteins into the cytosol of eukaryotic host cells, causing a broad spectrum of diseases including bacteremia, septicemia, typhoid fever, and bubonic plague in mammals, and localized lesions, systemic wilting, and blights in plants. In addition, type III secretion systems are also required for biogenesis of the bacterial flagellum. The HrcQ(B) protein, a component of the secretion apparatus of Pseudomonas syringae with homologues in all type III systems, has a variable N-terminal and a conserved C-terminal domain (HrcQ(B)-C). Here, we report the crystal structure of HrcQ(B)-C and show that this domain retains the ability of the full-length protein to interact with other type III components. A 3D analysis of sequence conservation patterns reveals two clusters of residues potentially involved in protein–protein interactions. Based on the analogies between HrcQ(B) and its flagellum homologues, we propose that HrcQ(B)-C participates in the formation of a C-ring-like assembly.
|Copyright, Publisher and Additional Information:||© Copyright 2004 National Academy of Sciences, U.S.A.|
|Institution:||The University of Leeds|
|Academic Units:||The University of Leeds > University of Leeds Research Centres and Institutes > Astbury Centre for Structural Molecular Biology (Leeds)
The University of Leeds > Faculty of Biological Sciences (Leeds) > Institute of Molecular and Cellular Biology (Leeds)
|Depositing User:||Sherpa Assistant|
|Date Deposited:||13 Mar 2006|
|Last Modified:||08 Jun 2014 01:20|
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