Display Settings:

Format

Send to:

Choose Destination
    J Biol Chem. 2009 Mar 6;284(10):6403-13. Epub 2008 Dec 4.

    Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain.

    Source

    Department I, Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstrasse 35, 72076 Tübingen, Germany.

    Abstract

    Colicins are plasmid-encoded toxic proteins produced by Escherichia coli strains to kill other E. coli strains that lack the corresponding immunity protein. Colicins intrude into the host cell by exploiting existing transport, diffusion, or efflux systems. We have traced the way colicin S4 takes to execute its function and show that it interacts specifically with OmpW, OmpF, and the Tol system before it inserts its pore-forming domain into the cytoplasmic membrane. The common structural architecture of colicins comprises a translocation, a receptor-binding, and an activity domain. We have solved the crystal structure of colicin S4 to a resolution of 2.5 A, which shows a remarkably compact domain arrangement of four independent domains, including a unique domain duplication of the receptor-binding domain. Finally, we have determined the residues responsible for binding to the receptor OmpW by mutating exposed charged residues in one or both receptor-binding domains.

    PMID:
    19056731
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2649078
    Free PMC Article

    Images from this publication.See all images (6) Free text

    FIGURE 1.
    FIGURE 2.
    FIGURE 3.
    FIGURE 4.
    FIGURE 5.
    FIGURE 6.

      Supplemental Content

      Icon for HighWire Press Icon for PubMed Central

      Save items

      loading

      Structures reported by this article

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk