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TitleAssembly principles of a unique cage formed by hexameric and decameric E. coli proteins.
Journal, issue, pagesElife, Vol. 3, Page e03653, Year 2014
Publish dateAug 5, 2014
AuthorsHélène Malet / Kaiyin Liu / Majida El Bakkouri / Sze Wah Samuel Chan / Gregory Effantin / Maria Bacia / Walid A Houry / Irina Gutsche /
PubMed AbstractA 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 ...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.
External linksElife / PubMed:25097238 / PubMed Central
MethodsEM (single particle)
Resolution7.5 - 11.0 Å
Structure data

2679

4upb

EMDB-2679: Electron cryo-microscopy of the complex formed between the hexameric AAA+ ATPase RavA and the decameric inducible decarboxylase LdcI
PDB-4upb: Electron cryo-microscopy of the complex formed between the hexameric ATPase RavA and the decameric inducible decarboxylase LdcI
Method: EM (single particle) / Resolution: 11.0 Å

2681

4upf

EMDB-2681: Assembly principles of the unique cage formed by the AAA+ ATPase RavA hexamer and the lysine decarboxylase LdcI decamer
PDB-4upf: Assembly principles of the unique cage formed by the ATPase RavA hexamer and the lysine decarboxylase LdcI decamer
Method: EM (single particle) / Resolution: 7.5 Å

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli str. k-12 substr. mg1655 (bacteria)
KeywordsLYASE/HYDROLASE / LYASE-HYDROLASE COMPLEX / LYSINE DECARBOXYLASE / AAA+ ATPASE / BACTERIAL ACID STRESS / ACID STRESS RESPONSE

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