5NWL

Crystal structure of a human RAD51-ATP filament.

5NWL の概要

• エントリーDOI: 10.2210/pdb5nwl/pdb
• 分子名称: DNA repair protein RAD51 homolog 1, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: atpase, dna-strand exchange, homologous recombination, double-strand dna break repair, recombination
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus : Q06609
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 525568.55

構造登録者

Pellegrini, L.,Moschetti, T. (登録日: 2017-05-06, 公開日: 2018-03-07, 最終更新日: 2024-01-17)

主引用文献

Brouwer, I.,Moschetti, T.,Candelli, A.,Garcin, E.B.,Modesti, M.,Pellegrini, L.,Wuite, G.J.,Peterman, E.J.
Two distinct conformational states define the interaction of human RAD51-ATP with single-stranded DNA.
EMBO J., 37:-, 2018

PubMed Abstract: An essential mechanism for repairing DNA double-strand breaks is homologous recombination (HR). One of its core catalysts is human RAD51 (hRAD51), which assembles as a helical nucleoprotein filament on single-stranded DNA, promoting DNA-strand exchange. Here, we study the interaction of hRAD51 with single-stranded DNA using a single-molecule approach. We show that ATP-bound hRAD51 filaments can exist in two different states with different contour lengths and with a free-energy difference of ~4 kT per hRAD51 monomer. Upon ATP hydrolysis, the filaments convert into a disassembly-competent ADP-bound configuration. In agreement with the single-molecule analysis, we demonstrate the presence of two distinct protomer interfaces in the crystal structure of a hRAD51-ATP filament, providing a structural basis for the two conformational states of the filament. Together, our findings provide evidence that hRAD51-ATP filaments can exist in two interconvertible conformational states, which might be functionally relevant for DNA homology recognition and strand exchange.

PubMed: 29507080
DOI: 10.15252/embj.201798162

実験手法

X-RAY DIFFRACTION (3.93 Å)