Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
- CNRS, European Molecular Biology Laboratory, France
- University of Toronto, Canada
- CNRS, Université Grenoble Alpes, France
- CEA, CNRS, Université Grenoble Alpes, France
Abstract
A 3.3 MDa macromolecular cage between two E. coli proteins with seemingly incompatible symmetries - the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI - is reconstructed by cryo-electron microscopy to 11 Å resolution. Combined with a 7.5 Å resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily.
Article and author information
Author details
Reviewing Editor
- Sjors HW Scheres, Medical Research Council Laboratory of Molecular Biology, United Kingdom
Version history
- Received: June 11, 2014
- Accepted: July 28, 2014
- Accepted Manuscript published: August 5, 2014 (version 1)
- Version of Record published: August 29, 2014 (version 2)
Copyright
© 2014, Malet et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
eLife 3:e03653.
https://doi.org/10.7554/eLife.03653
Further reading
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- Physics of Living Systems
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