Structure of HrcQ(B)-C, a conserved component of the bacterial type III secretion systems

Article English OPEN
Fadouloglou, V.E. ; Tampakaki, A.P. ; Glykos, N.M. ; Bastaki, M.N ; Hadden, J.M. ; Phillips, S.E.V. ; Panopoulos, N.J. ; Kokkinidis, M. (2004)

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\ud 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\ud 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,\ud we propose that HrcQ(B)-C participates in the formation of\ud a C-ring-like assembly.
  • References (29)
    29 references, page 1 of 3

    1. Hueck, C. J. (1998) Microbiol. Mol. Biol. Rev. 62, 379-433.

    2. Alfano, J. R. & Collmer, A. (1997) J. Bacteriol. 179, 5655-5662.

    3. Gal´an, J. E. & Collmer, A. (1999) Science 284, 1322-1328.

    4. Bu¨ttner, D. & Bonas, U. (2000) EMBO J. 21, 5313-5322.

    5. Jin, Q. & He, S.-Y. (2001) Science 294, 2556-2558.

    6. Stebbins, C. E. & Gal´an, J. E. (2001) Nature 414, 77-81.

    7. Luo, Y., Bertero, M. G., Frey, E. A., Pfuetzner, R. A., Wenk, M. R., Creagh, L., Marcus, S. L., Lim, D., Sicheri, F., Kay, C., et al. (2001) Nat. Struct. Biol. 8, 1031-1036.

    8. Rossier, O., Wengelnik, K., Hahn, K. & Bonas, U. (1999) Proc. Natl. Acad. Sci. USA 96, 9368-9373.

    9. Collmer, A., Badel, J. L., Charkowski, A. O., Deng, W. L., Fouts, D. E., Ramos, A. R., Rehm, A. H., Anderson, D. M., Schneewind, O., van Dijk, K., et al. (2000) Proc. Natl. Acad. Sci. USA 97, 8770-8777.

    10. Anderson, D. M., Fouts, D. E., Collmer, A. & Schneewind, O. (1999) Proc. Natl. Acad. Sci. USA 96, 12839-12834.

  • Similar Research Results (1)
  • Bioentities (1)
    1o9y Protein Data Bank
  • Metrics
    views in OpenAIRE
    views in local repository
    downloads in local repository

    The information is available from the following content providers:

    From Number Of Views Number Of Downloads
    White Rose Research Online - IRUS-UK 0 12
Share - Bookmark