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

Vidya Chandran, Rémi Fronzes, Stéphane Duquerroy, Nora Cronin, Jorge Navaza and Gabriel Waksman ()
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Vidya Chandran: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Rémi Fronzes: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Stéphane Duquerroy: Institut Pasteur, Unité de Virologie Structurale, Paris, 25–28 Rue du Dr Roux, F-75724 Paris, France
Nora Cronin: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK
Jorge Navaza: Laboratoire de Microscopie Electronique, Institut de Biologie Structurale J.P. Ebel, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France
Gabriel Waksman: Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK

Nature, 2009, vol. 462, issue 7276, 1011-1015

Abstract: 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.

Date: 2009
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DOI: 10.1038/nature08588

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