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
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.
Metrics
-
- 2,752
- views
-
- 188
- downloads
-
- 20
- citations
Views, downloads and citations are aggregated across all versions of this paper published by eLife.
Citations by DOI
-
- 20
- citations for umbrella DOI https://doi.org/10.7554/eLife.03653
Download links
A two-part list of links to download the article, or parts of the article, in various formats.
Downloads (link to download the article as PDF)
Open citations (links to open the citations from this article in various online reference manager services)
Cite this article (links to download the citations from this article in formats compatible with various reference manager tools)
Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
eLife 3:e03653.
https://doi.org/10.7554/eLife.03653
