2fpk Citations

Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change.

Biochemistry 44 13753-61 (2005)
Related entries: 2fpl, 2fpm

Cited: 24 times
EuropePMC logo PMID: 16229465

Abstract

Members of a superfamily of RecA-like recombinases facilitate a central strand exchange reaction in the DNA repair process. Archaeal RadA and Rad51 and eukaryal Rad51 and meiosis-specific DMC1 form a closely related group of recombinases distinct from bacterial RecA. Nevertheless, all such recombinases share a conserved core domain which carries the ATPase site and putative DNA-binding sites. Here we present the crystal structure of an archaeal RadA from Methanococcus voltae (MvRadA) in complex with ADP and Mg2+ at 2.1 A resolution. The crystallized RadA-ADP filament has an extended helical pitch similar to those of previously determined structures in the presence of nonhydrolyzable ATP analogue AMP-PNP. Structural comparison reveals two recurrent conformations with an extensive allosteric effect spanning the ATPase site and the putative DNA-binding L2 region. Varied conformations of the L2 region also imply a dynamic nature of recombinase-bound DNA.

Articles - 2fpk mentioned but not cited (2)

  1. Inter-subunit interactions that coordinate Rad51's activities. Grigorescu AA, Vissers JH, Ristic D, Pigli YZ, Lynch TW, Wyman C, Rice PA. Nucleic Acids Res 37 557-567 (2009)
  2. ATP half-sites in RadA and RAD51 recombinases bind nucleotides. Marsh ME, Scott DE, Ehebauer MT, Abell C, Blundell TL, Hyvönen M. FEBS Open Bio 6 372-385 (2016)


Reviews citing this publication (4)

Articles citing this publication (18)