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Updated: Apr 26, 2026

Producing Gene Deletions in Escherichia coli by P1 Transduction with Excisable Antibiotic Resistance Cassettes
Published on: September 1, 2018
Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
Hélène Malet1, Kaiyin Liu2, Majida El Bakkouri2
1European Molecular Biology Laboratory, Grenoble, France Unit for Virus Host-Cell Interactions, Université Grenoble Alpes, Grenoble, France Unit for Virus Host-Cell Interactions, CNRS, Grenoble, France.
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.
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