3CMU
Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
Summary for 3CMU
Entry DOI | 10.2210/pdb3cmu/pdb |
Related | 3CMT 3CMV 3CMW 3CMX |
Descriptor | DNA (5'-D(*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DT)-3'), Protein recA, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | homologous recombination, recombination-dna complex, recombination/dna |
Biological source | Escherichia coli More |
Cellular location | Cytoplasm: P0A7G6 |
Total number of polymer chains | 2 |
Total formula weight | 227728.70 |
Authors | Pavletich, N.P. (deposition date: 2008-03-24, release date: 2008-05-20, Last modification date: 2024-02-21) |
Primary citation | Chen, Z.,Yang, H.,Pavletich, N.P. Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature, 453:489-494, 2008 Cited by PubMed Abstract: The RecA family of ATPases mediates homologous recombination, a reaction essential for maintaining genomic integrity and for generating genetic diversity. RecA, ATP and single-stranded DNA (ssDNA) form a helical filament that binds to double-stranded DNA (dsDNA), searches for homology, and then catalyses the exchange of the complementary strand, producing a new heteroduplex. Here we have solved the crystal structures of the Escherichia coli RecA-ssDNA and RecA-heteroduplex filaments. They show that ssDNA and ATP bind to RecA-RecA interfaces cooperatively, explaining the ATP dependency of DNA binding. The ATP gamma-phosphate is sensed across the RecA-RecA interface by two lysine residues that also stimulate ATP hydrolysis, providing a mechanism for DNA release. The DNA is underwound and stretched globally, but locally it adopts a B-DNA-like conformation that restricts the homology search to Watson-Crick-type base pairing. The complementary strand interacts primarily through base pairing, making heteroduplex formation strictly dependent on complementarity. The underwound, stretched filament conformation probably evolved to destabilize the donor duplex, freeing the complementary strand for homology sampling. PubMed: 18497818DOI: 10.1038/nature06971 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4.2 Å) |
Structure validation
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