3EW9

RADA recombinase from METHANOCOCCUS MARIPALUDIS in complex with AMPPNP and potassium ions

3EW9 の概要

• エントリーDOI: 10.2210/pdb3ew9/pdb
• 関連するPDBエントリー: 3ETL 3EWA
• 分子名称: DNA repair and recombination protein radA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: rada, strand exchange protein, atpase, recombinase, atp analogue, atp-binding, dna damage, dna recombination, dna-binding, nucleotide-binding, dna binding protein, recombination
• 由来する生物種: Methanococcus maripaludis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35838.17

構造登録者

Li, Y.,He, Y.,Luo, Y. (登録日: 2008-10-14, 公開日: 2009-05-05, 最終更新日: 2023-09-06)

主引用文献

Li, Y.,He, Y.,Luo, Y.
Conservation of a conformational switch in RadA recombinase from Methanococcus maripaludis.
Acta Crystallogr.,Sect.D, 65:602-610, 2009

PubMed Abstract: Archaeal RadAs are close homologues of eukaryal Rad51s ( approximately 40% sequence identity). These recombinases promote ATP hydrolysis and a hallmark strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. Pairing of the 3'-overhangs located at the damaged DNA with a homologous double-stranded DNA enables the re-synthesis of the damaged region using the homologous DNA as the template. In recent studies, conformational changes in the DNA-interacting regions of Methanococcus voltae RadA have been correlated with the presence of activity-stimulating potassium or calcium ions in the ATPase centre. The series of crystal structures of M. maripaludis RadA presented here further suggest the conservation of an allosteric switch in the ATPase centre which controls the conformational status of DNA-interacting loops. Structural comparison with the distant Escherichia coli RecA homologue supports the notion that the conserved Lys248 and Lys250 residues in RecA play a role similar to that of cations in RadA. The conservation of a cationic bridge between the DNA-interacting L2 region and the terminal phosphate of ATP, together with the apparent stability of the nucleoprotein filament, suggests a gap-displacement model which may explain the advantage of ATP hydrolysis for DNA-strand exchange.

PubMed: 19465774
DOI: 10.1107/S0907444909011871

実験手法

X-RAY DIFFRACTION (2.4 Å)