6SZA

MoxR AAA-ATPase RavA, C2-symmetric closed ring conformation

Summary for 6SZA

• Entry DOI: 10.2210/pdb6sza/pdb
• Related: 6Q7L 6Q7M 6SZB
• EMDB information: 10351
• Descriptor: RavA, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: aaa+ atpase, moxr, escherichia coli, chaperone
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 6
• Total formula weight: 340436.32

Authors

Jessop, M.,Felix, J.,Gutsche, I. (deposition date: 2019-10-02, release date: 2020-02-19, Last modification date: 2024-05-22)

Primary citation

Jessop, 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

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

Experimental method

ELECTRON MICROSCOPY (6 Å)