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J. Biol. Chem., Vol. 279, Issue 38, 39750-39756, September 17, 2004

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Structure of the Neisseria meningitidis Outer Membrane PilQ Secretin Complex at 12 Å Resolution^*

Richard F. Collins, Stephan A. Frye, Ashraf Kitmitto, Robert C. Ford, Tone Tønjum, and Jeremy P. Derrick¶

From the Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, Manchester M60 1QD, United Kingdom and the Centre for Molecular Biology and Neuroscience and the Institute of Microbiology, University of Oslo, Rikshospitalet, N-0027 Oslo, Norway

The bacterial pathogen Neisseria meningitidis expresses long, thin, retractile fibers (called type IV pili) from its cell surface and uses these adhesive structures to mediate primary attachment to epithelial cells during host colonization and invasion. PilQ is an outer membrane protein complex that is essential for the translocation of these pili across the outer membrane. Here, we present the structure of the PilQ complex determined by cryoelectron microscopy to 12 Å resolution. The dominant feature of the structure is a large central cavity, formed by four arm features that spiral upwards from a squared ring base and meet to form a prominent cap region. The cavity, running through the center of the complex, is continuous and is effectively sealed at both the top and bottom. Analysis of the complex using self-orientation and by examination of two-dimensional crystals indicates a strong C4 rotational symmetry, with a much weaker C12 rotational symmetry, consistent with PilQ possessing true C4 symmetry with C12 quasi-symmetry. We therefore suggest that the complex is a homododecamer, formed by association of 12 PilQ polypeptide chains into a tetramer of trimers. The structure of the PilQ complex, with its large and well defined central chamber, suggests that it may not function solely as a passive portal in the outer membrane, but could be actively involved in mediating pilus assembly or modification.

Received for publication, May 28, 2004 , and in revised form, July 14, 2004.

^* This work was supported by grants from the Wellcome Trust, the North of England Structural Biology Consortium (Biotechnology and Biological Sciences Research Council), and the Research Council of Norway. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Dept. of Biomolecular Sciences, UMIST, Sackville St., P. O. Box 88, Manchester M60 1QD, UK. Tel.: 44-161-200-4207; Fax: 44-161-236-0409; E-mail: Jeremy. Derrick{at}umist.ac.uk.

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