PAAR-repeat proteins sharpen and diversify the type VI secretion system spike

Mikhail M. Shneider, Sergey A. Buth, Brian T. Ho, Marek Basler, John J. Mekalanos () and Petr G. Leiman ()
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Mikhail M. Shneider: École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland
Sergey A. Buth: École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland
Brian T. Ho: Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA
Marek Basler: Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA
John J. Mekalanos: Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA
Petr G. Leiman: École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland

Nature, 2013, vol. 500, issue 7462, 350-353

Abstract: An X-ray structure of bacterial type VI secretion system components reveals that PAAR family proteins bind at the tip of the VgrG spike, providing new insights into the mechanisms of type VI secretion; experiments using bacteria confirmed the importance of PAAR proteins.

Date: 2013
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DOI: 10.1038/nature12453

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