3NBX
Crystal structure of E. coli RavA (Regulatory ATPase variant A) in complex with ADP
Summary for 3NBX
| Entry DOI | 10.2210/pdb3nbx/pdb |
| Descriptor | ATPase ravA, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | aaa+ atpase, alpha-beta-alpha structure, rossmann fold, hydrolase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P31473 |
| Total number of polymer chains | 1 |
| Total formula weight | 57166.10 |
| Authors | El Bakkouri, M. (deposition date: 2010-06-04, release date: 2011-01-12, Last modification date: 2024-02-21) |
| Primary citation | El Bakkouri, M.,Gutsche, I.,Kanjee, U.,Zhao, B.,Yu, M.,Goret, G.,Schoehn, G.,Burmeister, W.P.,Houry, W.A. Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity Proc.Natl.Acad.Sci.USA, 107:22499-22504, 2010 Cited by PubMed Abstract: The MoxR family of AAA+ ATPases is widespread throughout bacteria and archaea but remains poorly characterized. We recently found that the Escherichia coli MoxR protein, RavA (Regulatory ATPase variant A), tightly interacts with the inducible lysine decarboxylase, LdcI/CadA, to form a unique cage-like structure. Here, we present the X-ray structure of RavA and show that the αβα and all-α subdomains in the RavA AAA+ module are arranged as in magnesium chelatases rather than as in classical AAA+ proteins. RavA structure also contains a discontinuous triple-helical domain as well as a β-barrel-like domain forming a unique fold, which we termed the LARA domain. The LARA domain was found to mediate the interaction between RavA and LdcI. The RavA structure provides insights into how five RavA hexamers interact with two LdcI decamers to form the RavA-LdcI cage-like structure. PubMed: 21148420DOI: 10.1073/pnas.1009092107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.91 Å) |
Structure validation
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