7X5B

Crystal structure of RuvB

Summary for 7X5B

• Entry DOI: 10.2210/pdb7x5b/pdb
• Descriptor: Holliday junction ATP-dependent DNA helicase RuvB, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: ruvb, holliday juncition, homologous recombination, dna damage repair, atp hydrolysis, motor protein
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 1
• Total formula weight: 39394.75

Authors

Lin, Z.,Qu, Q.,Zhang, X.,Zhou, Z.,Dai, L. (deposition date: 2022-03-04, release date: 2023-03-08, Last modification date: 2023-11-29)

Primary citation

Zhang, X.,Zhou, Z.,Dai, L.,Chao, Y.,Liu, Z.,Huang, M.,Qu, Q.,Lin, Z.
Cryo-EM structure of the RuvAB-Holliday junction intermediate complex from Pseudomonas aeruginosa.
Front Plant Sci, 14:1139106-1139106, 2023

PubMed Abstract: Holliday junction (HJ) is a four-way structured DNA intermediate in homologous recombination. In bacteria, the HJ-specific binding protein RuvA and the motor protein RuvB together form the RuvAB complex to catalyze HJ branch migration. (, Pa) is a ubiquitous opportunistic bacterial pathogen that can cause serious infection in a variety of host species, including vertebrate animals, insects and plants. Here, we describe the cryo-Electron Microscopy (cryo-EM) structure of the RuvAB-HJ intermediate complex from . The structure shows that two RuvA tetramers sandwich HJ at the junction center and disrupt base pairs at the branch points of RuvB-free HJ arms. Eight RuvB subunits are recruited by the RuvA octameric core and form two open-rings to encircle two opposite HJ arms. Each RuvB subunit individually binds a RuvA domain III. The four RuvB subunits within the ring display distinct subdomain conformations, and two of them engage the central DNA duplex at both strands with their C-terminal β-hairpins. Together with the biochemical analyses, our structure implicates a potential mechanism of RuvB motor assembly onto HJ DNA.

PubMed: 37025142
DOI: 10.3389/fpls.2023.1139106

Experimental method

X-RAY DIFFRACTION (2.16 Å)