Summary for 2FPL
Entry DOI | 10.2210/pdb2fpl/pdb |
Related | 1T4G 1XU4 2FPK 2FPM |
Descriptor | DNA repair and recombination protein radA, MAGNESIUM ION, POTASSIUM ION, ... (5 entities in total) |
Functional Keywords | atpase, protein-atp complex, rada-adp complex, co-factors, potassium-dependence, recombination |
Biological source | Methanococcus voltae |
Total number of polymer chains | 1 |
Total formula weight | 35871.03 |
Authors | Wu, Y.,Qian, X.,He, Y.,Moya, I.A.,Luo, Y. (deposition date: 2006-01-16, release date: 2006-01-31, Last modification date: 2023-08-30) |
Primary citation | Qian, X.,Wu, Y.,He, Y.,Moya, I.A.,Luo, Y. Crystal Structure of Methanococcus Voltae Rada in Complex with Adp: hydrolysis-induced conformational change Biochemistry, 44:13753-13761, 2005 Cited by PubMed 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. PubMed: 16229465DOI: 10.1021/bi051222i PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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