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6Q7M

Spiral structure of E. coli RavA in the RavA-LdcI cage-like complex

This is a non-PDB format compatible entry.
Summary for 6Q7M
Entry DOI10.2210/pdb6q7m/pdb
EMDB information2679 4469 4470
DescriptorInducible lysine decarboxylase, ATPase RavA, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
Functional Keywordscomplex, moxr atpase, lysine decarboxylase, hydrolase
Biological sourceEscherichia coli
More
Total number of polymer chains26
Total formula weight1972327.68
Authors
Arragain, B.,Felix, J.,Malet, H.,Gutsche, I.,Jessop, M. (deposition date: 2018-12-13, release date: 2020-02-12, Last modification date: 2025-04-09)
Primary citationJessop, M.,Arragain, B.,Miras, R.,Fraudeau, A.,Huard, K.,Bacia-Verloop, M.,Catty, P.,Felix, J.,Malet, H.,Gutsche, I.
Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.
Commun Biol, 3:46-46, 2020
Cited by
PubMed Abstract: The hexameric MoxR AAA+ ATPase RavA and the decameric lysine decarboxylase LdcI form a 3.3 MDa cage, proposed to assist assembly of specific respiratory complexes in E. coli. Here, we show that inside the LdcI-RavA cage, RavA hexamers adopt an asymmetric spiral conformation in which the nucleotide-free seam is constrained to two opposite orientations. Cryo-EM reconstructions of free RavA reveal two co-existing structural states: an asymmetric spiral, and a flat C2-symmetric closed ring characterised by two nucleotide-free seams. The closed ring RavA state bears close structural similarity to the pseudo two-fold symmetric crystal structure of the AAA+ unfoldase ClpX, suggesting a common ATPase mechanism. Based on these structures, and in light of the current knowledge regarding AAA+ ATPases, we propose different scenarios for the ATP hydrolysis cycle of free RavA and the LdcI-RavA cage-like complex, and extend the comparison to other AAA+ ATPases of clade 7.
PubMed: 31992852
DOI: 10.1038/s42003-020-0772-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.8 Å)
Structure validation

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