1o9y
From Proteopedia
Crystal structure of the C-terminal domain of the HrcQb protein from Pseudomonas syringae pv. phaseolicola
Structural highlights
FunctionHRCQB_PSESH Component of the type III secretion system, which is required for effector protein delivery, parasitism, and pathogenicity. Probably participates in the formation of a C-ring-like assembly along with HrcQa. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedType 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. Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems.,Fadouloglou VE, Tampakaki AP, Glykos NM, Bastaki MN, Hadden JM, Phillips SE, Panopoulos NJ, Kokkinidis M Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):70-5. Epub 2003 Dec 23. PMID:14694203[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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