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2FPL

RadA recombinase in complex with AMP-PNP and low concentration of K+

Replaces:  1Z4C
Summary for 2FPL
Entry DOI10.2210/pdb2fpl/pdb
Related1T4G 1XU4 2FPK 2FPM
DescriptorDNA repair and recombination protein radA, MAGNESIUM ION, POTASSIUM ION, ... (5 entities in total)
Functional Keywordsatpase, protein-atp complex, rada-adp complex, co-factors, potassium-dependence, recombination
Biological sourceMethanococcus voltae
Total number of polymer chains1
Total formula weight35871.03
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 citationQian, 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: 16229465
DOI: 10.1021/bi051222i
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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