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Structure of the Type VI Secretion System Contractile Sheath

Kudryashev, Mikhail and Wang, Ray Yu-Ruei and Brackmann, Maximilian and Scherer, Sebastian and Maier, Timm and Baker, David and DiMaio, Frank and Stahlberg, Henning and Egelman, Edward H. and Basler, Marek. (2015) Structure of the Type VI Secretion System Contractile Sheath. Cell, Vol. 160, H. 5. pp. 952-962.

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Official URL: http://edoc.unibas.ch/dok/A6338895

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Abstract

Bacteria use rapid contraction of a long sheath of the type VI secretion system (T6SS) to deliver effectors into a target cell. Here, we present an atomic-resolution structure of a native contracted Vibrio cholerae sheath determined by cryo-electron microscopy. The sheath subunits, composed of tightly interacting proteins VipA and VipB, assemble into a six-start helix. The helix is stabilized by a core domain assembled from four β strands donated by one VipA and two VipB molecules. The fold of inner and middle layers is conserved between T6SS and phage sheaths. However, the structure of the outer layer is distinct and suggests a mechanism of interaction of the bacterial sheath with an accessory ATPase, ClpV, that facilitates multiple rounds of effector delivery. Our results provide a mechanistic insight into assembly of contractile nanomachines that bacteria and phages use to translocate macromolecules across membranes.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Infection Biology > Infection Biology (Basler)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning and Basler, Marek and Kudryashev, Mikhail and Brackmann, Maximilian and Maier, Timm and Scherer, Sebastian
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Cell Press
ISSN:0092-8674
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:10 Apr 2015 09:12
Deposited On:10 Apr 2015 09:12

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