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3VU9

Crystal Structure of Psy3-Csm2 complex

Summary for 3VU9
Entry DOI10.2210/pdb3vu9/pdb
DescriptorPlatinum sensitivity protein 3, Chromosome segregation in meiosis protein 2, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsdna repair, recombination, meiosis, dna binding protein
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
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Cellular locationNucleus : Q12318
Cytoplasm : P40465
Total number of polymer chains2
Total formula weight53673.88
Authors
Tawaramoto, M.,Sasanuma, H.,Hosaka, H.,Lao, J.P.,Sanda, E.,Suzuki, M.,Yamashita, E.,Hunter, N.,Shinohara, M.,Nakagawa, A.,Shinohara, A. (deposition date: 2012-06-23, release date: 2013-04-10, Last modification date: 2024-03-20)
Primary citationSasanuma, H.,Tawaramoto, M.S.,Lao, J.P.,Hosaka, H.,Sanda, E.,Suzuki, M.,Yamashita, E.,Hunter, N.,Shinohara, M.,Nakagawa, A.,Shinohara, A.
A new protein complex promoting the assembly of Rad51 filaments
Nat Commun, 4:1676-1676, 2013
Cited by
PubMed Abstract: During homologous recombination, eukaryotic RecA homologue Rad51 assembles into a nucleoprotein filament on single-stranded DNA to catalyse homologous pairing and DNA-strand exchange with a homologous template. Rad51 nucleoprotein filaments are highly dynamic and regulated via the coordinated actions of various accessory proteins including Rad51 mediators. Here, we identify a new Rad51 mediator complex. The PCSS complex, comprising budding yeast Psy3, Csm2, Shu1 and Shu2 proteins, binds to recombination sites and is required for Rad51 assembly and function during meiosis. Within the hetero-tetramer, Psy3-Csm2 constitutes a core sub-complex with DNA-binding activity. In vitro, purified Psy3-Csm2 stabilizes the Rad51-single-stranded DNA complex independently of nucleotide cofactor. The mechanism of Rad51 stabilization is inferred by our high-resolution crystal structure, which reveals Psy3-Csm2 to be a structural mimic of the Rad51-dimer, a fundamental unit of the Rad51-filament. Together, these results reveal a novel molecular mechanism for this class of Rad51-mediators, which includes the human Rad51 paralogues.
PubMed: 23575680
DOI: 10.1038/ncomms2678
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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