3NTU

RADA RECOMBINASE D302K MUTANT IN COMPLEX with AMP-PNP

Summary for 3NTU

• Entry DOI: 10.2210/pdb3ntu/pdb
• Related: 1T4G 2I1Q
• Descriptor: DNA repair and recombination protein radA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: atpase, recombinase, atp complex, active conformation, reca, rad51, dmc1, rada, recombination
• Biological source: Methanococcus voltae
• Total number of polymer chains: 1
• Total formula weight: 35430.43

Authors

Luo, Y. (deposition date: 2010-07-05, release date: 2011-07-27, Last modification date: 2023-09-06)

Primary citation

Amunugama, R.,He, Y.,Willcox, S.,Forties, R.A.,Shim, K.S.,Bundschuh, R.,Luo, Y.,Griffith, J.,Fishel, R.
RAD51 protein ATP cap regulates nucleoprotein filament stability.
J.Biol.Chem., 287:8724-8736, 2012

PubMed Abstract: RAD51 mediates homologous recombination by forming an active DNA nucleoprotein filament (NPF). A conserved aspartate that forms a salt bridge with the ATP γ-phosphate is found at the nucleotide-binding interface between RAD51 subunits of the NPF known as the ATP cap. The salt bridge accounts for the nonphysiological cation(s) required to fully activate the RAD51 NPF. In contrast, RecA homologs and most RAD51 paralogs contain a conserved lysine at the analogous structural position. We demonstrate that substitution of human RAD51(Asp-316) with lysine (HsRAD51(D316K)) decreases NPF turnover and facilitates considerably improved recombinase functions. Structural analysis shows that archaebacterial Methanococcus voltae RadA(D302K) (MvRAD51(D302K)) and HsRAD51(D316K) form extended active NPFs without salt. These studies suggest that the HsRAD51(Asp-316) salt bridge may function as a conformational sensor that enhances turnover at the expense of recombinase activity.

PubMed: 22275364
DOI: 10.1074/jbc.M111.239426

Experimental method

X-RAY DIFFRACTION (1.9 Å)