5H1C

Human RAD51 post-synaptic complexes

Summary for 5H1C

• Entry DOI: 10.2210/pdb5h1c/pdb
• Related: 5H1B
• EMDB information: 9566 9567 9568
• Descriptor: DNA repair protein RAD51 homolog 1, DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), DNA (5'-D(P*AP*AP*AP*AP*AP*AP*AP*AP*A)-3'), ... (5 entities in total)
• Functional Keywords: dna repair, atpase, homologous recombination, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q06609
• Total number of polymer chains: 5
• Total formula weight: 118082.41

Authors

Xu, J.,Zhao, L.,Xu, Y.,Zhao, W.,Sung, P.,Wang, H.W. (deposition date: 2016-10-08, release date: 2016-12-21, Last modification date: 2024-10-09)

Primary citation

Xu, J.,Zhao, L.,Xu, Y.,Zhao, W.,Sung, P.,Wang, H.W.
Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange
Nat. Struct. Mol. Biol., 24:40-46, 2017

PubMed Abstract: The central step in eukaryotic homologous recombination (HR) is ATP-dependent DNA-strand exchange mediated by the Rad51 recombinase. In this process, Rad51 assembles on single-stranded DNA (ssDNA) and generates a helical filament that is able to search for and invade homologous double-stranded DNA (dsDNA), thus leading to strand separation and formation of new base pairs between the initiating ssDNA and the complementary strand within the duplex. Here, we used cryo-EM to solve the structures of human RAD51 in complex with DNA molecules, in presynaptic and postsynaptic states, at near-atomic resolution. Our structures reveal both conserved and distinct structural features of the human RAD51-DNA complexes compared with their prokaryotic counterpart. Notably, we also captured the structure of an arrested synaptic complex. Our results provide new insight into the molecular mechanisms of the DNA homology search and strand-exchange processes.

PubMed: 27941862
DOI: 10.1038/nsmb.3336

Experimental method

ELECTRON MICROSCOPY (4.5 Å)