4UPB
Electron cryo-microscopy of the complex formed between the hexameric ATPase RavA and the decameric inducible decarboxylase LdcI
Summary for 4UPB
| Entry DOI | 10.2210/pdb4upb/pdb |
| EMDB information | 2679 |
| Descriptor | LYSINE DECARBOXYLASE, INDUCIBLE, ATPASE RAVA (2 entities in total) |
| Functional Keywords | lyase-hydrolase complex, lysine decarboxylase, aaa+ atpase, bacterial acid stress, lyase/hydrolase |
| Biological source | ESCHERICHIA COLI K-12 More |
| Cellular location | Cytoplasm : P0A9H3 P31473 |
| Total number of polymer chains | 5 |
| Total formula weight | 332642.52 |
| Authors | Malet, H.,Liu, K.,El Bakkouri, M.,Chan, S.W.S.,Effantin, G.,Bacia, M.,Houry, W.A.,Gutsche, I. (deposition date: 2014-06-15, release date: 2014-08-20, Last modification date: 2024-05-08) |
| Primary citation | Malet, H.,Liu, K.,El Bakkouri, M.,Chan, S.W.S.,Effantin, G.,Bacia, M.,Houry, W.A.,Gutsche, I. Assembly Principles of a Unique Cage Formed by Hexameric and Decameric E. Coli Proteins. Elife, 3:03653-, 2014 Cited by 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 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. PubMed: 25097238DOI: 10.7554/ELIFE.03653 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (11 Å) |
Structure validation
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