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• W2022685937 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." @default.
• W2022685937 created "2016-06-24" @default.
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• W2022685937 date "2012-04-20" @default.
• W2022685937 modified "2023-09-25" @default.
• W2022685937 title "Structure of a hexameric form of RadA recombinase from<i>Methanococcus voltae</i>" @default.
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• W2022685937 doi "https://doi.org/10.1107/s1744309112010226" @default.
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