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Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state

Eifler, N. and Vetsch, M. and Gregorini, M. and Ringler, P. and Chami, M. and Philippsen, A. and Fritz, A. and Muller, S. A. and Glockshuber, R. and Engel, A. and Grauschopf, U.. (2006) Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state. The EMBO journal, Vol. 25, H. 11. pp. 2652-2661.

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Official URL: http://edoc.unibas.ch/dok/A5262469

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Abstract

ClyA is a pore-forming toxin from virulent Escherichia coli and Salmonella enterica strains. Here, we show that the intrinsic hemolytic activity of ClyA is independent of its redox state, and that the assembly of both reduced and oxidized ClyA to the ring-shaped oligomer is triggered by contact with lipid or detergent. A rate-limiting conformational transition in membrane-bound ClyA monomers precedes their assembly to the functional pore. We obtained a three-dimensional model of the detergent-induced oligomeric complex at 12 A resolution by combining cryo- and negative stain electron microscopy with mass measurements by scanning transmission electron microscopy. The model reveals that 13 ClyA monomers assemble into a cylinder with a hydrophobic cap region, which may be critical for membrane insertion. [on SciFinder (R)]
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H and Ringler, Philippe and Müller, Shirley
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:0261-4189
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:14 Sep 2012 06:50
Deposited On:22 Mar 2012 13:24

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