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Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.

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.

SUBMITTER: Malet H

PROVIDER: S-EPMC4145799 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.

Malet Hélène H Liu Kaiyin K El Bakkouri Majida M Chan Sze Wah Samuel SW Effantin Gregory G Bacia Maria M Houry Walid A WA Gutsche Irina I

eLife 20140805

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 pseudoato ...[more]

PMID: 25097238

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