2GDJ

Delta-62 RADA recombinase in complex with AMP-PNP and magnesium

Summary for 2GDJ

• Entry DOI: 10.2210/pdb2gdj/pdb
• Related: 1T4G
• Descriptor: DNA repair and recombination protein radA, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• Functional Keywords: atpase, protein-atp complex, recombination
• Biological source: Methanococcus voltae
• Total number of polymer chains: 1
• Total formula weight: 29720.83

Authors

Wu, Y.,Qian, X.,He, Y.,Luo, Y. (deposition date: 2006-03-16, release date: 2006-05-16, Last modification date: 2023-08-30)

Primary citation

Galkin, V.E.,Wu, Y.,Zhang, X.-P.,Qian, X.,He, Y.,Yu, X.,Heyer, W.-D.,Luo, Y.,Egelman, E.H.
The Rad51/RadA N-Terminal Domain Activates Nucleoprotein Filament ATPase Activity.
Structure, 14:983-992, 2006

PubMed Abstract: Proteins in the RecA/RadA/Rad51 family form helical filaments on DNA that function in homologous recombination. While these proteins all have the same highly conserved ATP binding core, the RadA/Rad51 proteins have an N-terminal domain that shows no homology with the C-terminal domain found in RecA. Both the Rad51 N-terminal and RecA C-terminal domains have been shown to bind DNA, but no role for these domains has been established. We show that RadA filaments can be trapped in either an inactive or active conformation with respect to the ATPase and that activation involves a large rotation of the subunit aided by the N-terminal domain. The G103E mutation within the yeast Rad51 N-terminal domain inactivates the filament by failing to make proper contacts between the N-terminal domain and the core. These results show that the N-terminal domains play a regulatory role in filament activation and highlight the modular architecture of the recombination proteins.

PubMed: 16765891
DOI: 10.1016/j.str.2006.04.001

Experimental method

X-RAY DIFFRACTION (2.5 Å)