3CMW
Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
3CMW の概要
エントリーDOI | 10.2210/pdb3cmw/pdb |
関連するPDBエントリー | 3CMT 3CMU 3CMV 3CMX |
分子名称 | DNA (5'-D(*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DTP*DT)-3'), Protein recA, MAGNESIUM ION, ... (5 entities in total) |
機能のキーワード | homologous recombination, recombination-dna complex, recombination/dna |
由来する生物種 | Escherichia coli 詳細 |
細胞内の位置 | Cytoplasm: P0A7G6 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 379061.99 |
構造登録者 | |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード