4DC9

Hexameric ring of Methanococcus voltae RadA

Summary for 4DC9

• Entry DOI: 10.2210/pdb4dc9/pdb
• Related: 1T4G
• Descriptor: DNA repair and recombination protein radA, NITRATE ION (3 entities in total)
• Functional Keywords: hexamer, rada, recombinase, homologous recombination, reca, dna binding protein
• Biological source: Methanococcus voltae
• Total number of polymer chains: 6
• Total formula weight: 177109.70

Authors

Du, L.,Luo, Y. (deposition date: 2012-01-17, release date: 2012-05-02, Last modification date: 2023-09-13)

Primary citation

Du, L.,Luo, Y.
Structure of a hexameric form of RadA recombinase from Methanococcus voltae.
Acta Crystallogr.,Sect.F, 68:511-516, 2012

PubMed Abstract: Archaeal RadA proteins are close homologues of eukaryal Rad51 and DMC1 proteins and are remote homologues of bacterial RecA proteins. For the repair of double-stranded breaks in DNA, these recombinases promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. This DNA-repair function also plays a key role in the resistance of cancer cells to chemotherapy and radiotherapy and in the resistance of bacterial cells to antibiotics. A hexameric form of a truncated Methanococcus voltae RadA protein devoid of its small N-terminal domain has been crystallized. The RadA hexamers further assemble into two-ringed assemblies. Similar assemblies can be observed in the crystals of Pyrococcus furiosus RadA and Homo sapiens DMC1. In all of these two-ringed assemblies the DNA-interacting L1 region of each protomer points inward towards the centre, creating a highly positively charged locus. The electrostatic characteristics of the central channels can be utilized in the design of novel recombinase inhibitors.

PubMed: 22691778
DOI: 10.1107/S1744309112010226

Experimental method

X-RAY DIFFRACTION (2.6 Å)