Double hexameric ring assembly of the type III protein translocase ATPase HrcN

doi:10.1111/j.1365-2958.2006.05219.x

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Wiley InterScience

Molecular Microbiology

Volume 61 Issue 1, Pages 119 - 125

Published Online: 1 Jun 2006

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Double hexameric ring assembly of the type III protein translocase ATPase HrcN

Shirley A. Müller, ¹ Charalambos Pozidis, ²
Remington Stone, ³ Christian Meesters, ³
Mohamed Chami, ¹ Andreas Engel, ¹
Anastassios Economou ² and Henning Stahlberg ³ *

¹ M. E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
² Institute of Molecular Biology and Biotechnology, FORTH and Department of Biology, University of Crete, PO Box 1527, GR-711 10 Iraklio, Crete, Greece.
³ Molecular and Cellular Biology, University of California at Davis, 1 Shields Avenue, Davis, CA 95616, USA.

Correspondence to *E-mail hstahlberg@ucdavis.edu; Tel. (+1) 530 752 8282; Fax (+1) 530 752 3085.

ABSTRACT

The specialized type III secretion (T3S) apparatus of pathogenic and symbiotic Gram-negative bacteria comprises a complex transmembrane organelle and an ATPase homologous to the F₁-ATPase β subunit. The T3S ATPase HrcN of Pseudomonas syringae associates with the inner membrane, and its ATP hydrolytic activity is stimulated by dodecamerization. The structure of dodecameric HrcN (HrcN₁₂) determined to 1.6 nm by cryo-electron microscopy is presented. HrcN₁₂ comprises two hexameric rings that are probably stacked face-to-face by the association of their C-terminal domains. It is 11.5 ± 1.0 nm in diameter, 12.0 ± 2.0 nm high and has a 2.0–3.8 nm wide inner channel. This structure is compared to a homology model based on the structure of the F₁-β-ATPase. A model for its incorporation within the T3S apparatus is presented.

Accepted 2 May, 2006.

DIGITAL OBJECT IDENTIFIER (DOI)

10.1111/j.1365-2958.2006.05219.x About DOI