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3CMU

Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures

Summary for 3CMU
Entry DOI10.2210/pdb3cmu/pdb
Related3CMT 3CMV 3CMW 3CMX
DescriptorDNA (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 Keywordshomologous recombination, recombination-dna complex, recombination/dna
Biological sourceEscherichia coli
More
Cellular locationCytoplasm: P0A7G6
Total number of polymer chains2
Total formula weight227728.70
Authors
Pavletich, N.P. (deposition date: 2008-03-24, release date: 2008-05-20, Last modification date: 2024-02-21)
Primary citationChen, 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: 18497818
DOI: 10.1038/nature06971
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.2 Å)
Structure validation

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