4A6P

RadA C-terminal ATPase domain from Pyrococcus furiosus

4A6P の概要

• エントリーDOI: 10.2210/pdb4a6p/pdb
• 関連するPDBエントリー: 1PZN
• 分子名称: DNA REPAIR AND RECOMBINATION PROTEIN RADA, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: hydrolase, recombinase
• 由来する生物種: PYROCOCCUS FURIOSUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25605.12

構造登録者

Marsh, M.E.,Ehebauer, M.T.,Scott, D.,Abell, C.,Blundell, T.L.,Hyvonen, M. (登録日: 2011-11-08, 公開日: 2012-11-14, 最終更新日: 2023-12-20)

主引用文献

Marsh, M.E.,Scott, D.E.,Ehebauer, M.T.,Abell, C.,Blundell, T.L.,Hyvonen, M.
ATP Half-Sites in Rada and Rad51 Recombinases Bind Nucleotides
FEBS Open Bio, 6:372-, 2016

PubMed Abstract: Homologous recombination is essential for repair of DNA double-strand breaks. Central to this process is a family of recombinases, including archeal RadA and human RAD51, which form nucleoprotein filaments on damaged single-stranded DNA ends and facilitate their ATP-dependent repair. ATP binding and hydrolysis are dependent on the formation of a nucleoprotein filament comprising RadA/RAD51 and single-stranded DNA, with ATP bound between adjacent protomers. We demonstrate that truncated, monomeric Pyrococcus furiosus RadA and monomerised human RAD51 retain the ability to bind ATP and other nucleotides with high affinity. We present crystal structures of both apo and nucleotide-bound forms of monomeric RadA. These structures reveal that while phosphate groups are tightly bound, RadA presents a shallow, poorly defined binding surface for the nitrogenous bases of nucleotides. We suggest that RadA monomers would be constitutively bound to nucleotides in the cell and that the bound nucleotide might play a structural role in filament assembly.

PubMed: 27419043
DOI: 10.1002/2211-5463.12052

実験手法

X-RAY DIFFRACTION (1.498 Å)