Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 25097238.
- Also identified by DOI 10.7554/eLife.03653 and PMC identifier 4145799.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
A 3.3 MDa macromolecular cage between two Escherichia 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.
Medical subject headings
- Adenosine Triphosphatases
- Carboxy-Lyases
- Escherichia coli
- Escherichia coli Proteins