Skip NavigationSkip to Content
Return Return to Search Results

Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis

  1. Author:
    Evdokimov, A. G.
    Tropea, J. E.
    Routzahn, K. M.
    Waugh, D. S.

  2. Author Address

    NCI, Macromol Crystallog Lab, Ctr Canc Res, POB B, Frederick, MD 21702 USA. NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA. Waugh DS NCI, Macromol Crystallog Lab, Ctr Canc Res, POB B, Frederick, MD 21702 USA.
    1. Year: 2002
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 58
    2. Part 3
    3. Pages: 398-406
  4. Type of Article: Article
  1. Abstract:

    Many bacterial pathogens utilize a type III (contact-dependent) secretion system to inject cytotoxic effector proteins directly into host cells. This ingenious mechanism, designed for both bacterial offense and defense, has been studied most extensively in Yersinia spp. To be exported efficiently, at least three of the effectors (YopE, YopH and YopT) and several other proteins that transit the type III secretion pathway in Yersinia (YopN, YopD and YopB) must first form transient complexes with cognate-specific Yop chaperone (Syc) proteins. The cytotoxic effector YopE, a selective activator of mammalian Rho-family GTPases, associates with SycE. Here, the structure of Y. pestis SycE at 1.95 Angstrom resolution is reported. SycE possesses a novel fold with an unusual dimerization motif and an intriguing basic cavity located on the dyad axis of the dimer that may participate in its interaction with YopE.

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel