1O9Y

Crystal structure of the C-terminal domain of the HrcQb protein from Pseudomonas syringae pv. phaseolicola

Summary for 1O9Y

• Entry DOI: 10.2210/pdb1o9y/pdb
• Descriptor: HRCQ2 (2 entities in total)
• Functional Keywords: secretory protein, hrp, type iii secretion system, phytopathogenicity, structural protein
• Biological source: PSEUDOMONAS SYRINGAE
• Cellular location: Cytoplasm: O85094
• Total number of polymer chains: 4
• Total formula weight: 35812.73

Authors

Fadouloglou, V.E.,Kokkinidis, M. (deposition date: 2002-12-20, release date: 2003-12-04, Last modification date: 2024-11-20)

Primary citation

Fadouloglou, V.E.,Tampakaki, A.P.,Glykos, N.M.,Bastaki, M.N.,Hadden, J.M.,Phillips, S.E.,Panopoulos, N.J.,Kokkinidis, M.
Structure of Hrcqb-C, a Conserved Component of the Bacterial Type III Secretion Systems.
Proc.Natl.Acad.Sci.USA, 101:70-, 2004

PubMed Abstract: 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.

PubMed: 14694203
DOI: 10.1073/PNAS.0304579101

Experimental method

X-RAY DIFFRACTION (2.29 Å)