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-Structure paper
Title | Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. |
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Journal, issue, pages | Elife, Vol. 3, Page e03653, Year 2014 |
Publish date | Aug 5, 2014 |
Authors | Hélène Malet / Kaiyin Liu / Majida El Bakkouri / Sze Wah Samuel Chan / Gregory Effantin / Maria Bacia / Walid A Houry / Irina Gutsche / |
PubMed 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 ...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 links | Elife / PubMed:25097238 / PubMed Central |
Methods | EM (single particle) |
Resolution | 7.5 - 11.0 Å |
Structure data | EMDB-2679: Electron cryo-microscopy of the complex formed between the hexameric AAA+ ATPase RavA and the decameric inducible decarboxylase LdcI EMDB-2681: Assembly principles of the unique cage formed by the AAA+ ATPase RavA hexamer and the lysine decarboxylase LdcI decamer |
Source |
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Keywords | LYASE/HYDROLASE / LYASE-HYDROLASE COMPLEX / LYSINE DECARBOXYLASE / AAA+ ATPASE / BACTERIAL ACID STRESS / ACID STRESS RESPONSE |