2fpm
RadA recombinase in complex with AMP-PNP and high concentration of K+
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OverviewOverview
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.
About this StructureAbout this Structure
2FPM is a Single protein structure of sequence from Methanococcus voltae with , and as ligands. This structure supersedes the now removed PDB entry 1Z4D. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change., Qian X, Wu Y, He Y, Luo Y, Biochemistry. 2005 Oct 25;44(42):13753-61. PMID:16229465
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