BIROn - Birkbeck Institutional Research Online

    Structure of the outer membrane complex of a type IV secretion system

    Chandran, Vidya and Duquerroy, S. and Cronin, Nora and Navaza, J. and Fronzes, Remi and Waksman, Gabriel (2009) Structure of the outer membrane complex of a type IV secretion system. Nature 462 (7276), pp. 1011-1015. ISSN 0028-0836.

    Full text not available from this repository.

    Abstract

    Type IV secretion systems are secretion nanomachines spanning the two membranes of Gram-negative bacteria. Three proteins, VirB7, VirB9 and VirB10, assemble into a 1.05 megadalton (MDa) core spanning the inner and outer membranes. This core consists of 14 copies of each of the proteins and forms two layers, the I and O layers, inserting in the inner and outer membrane, respectively. Here we present the crystal structure of a ~0.6 MDa outer-membrane complex containing the entire O layer. This structure is the largest determined for an outer-membrane channel and is unprecedented in being composed of three proteins. Unexpectedly, this structure identifies VirB10 as the outer-membrane channel with a unique hydrophobic double-helical transmembrane region. This structure establishes VirB10 as the only known protein crossing both membranes of Gram-negative bacteria. Comparison of the cryo-electron microscopy (cryo-EM) and crystallographic structures points to conformational changes regulating channel opening and closing.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 04 Aug 2010 14:09
    Last Modified: 06 Dec 2016 10:46
    URI: http://eprints.bbk.ac.uk/id/eprint/1175

    Statistics

    Downloads
    Activity Overview
    0Downloads
    89Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item