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Literature summary for 3.6.4.B7 extracted from
- Structure of a hexameric form of RadA recombinase from Methanococcus voltae (2012), Acta Crystallogr. Sect. F, 68, 511-516.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Methanococcus voltae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallization of a hexameric form of a truncated Methanococcus voltae RadA protein devoid of its small N-terminal domain, crystals are grown by the hanging drop method The RadA hexamers further assemble into two-ringed assemblies | Methanococcus voltae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanococcus voltae | O73948 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RadA | - |
Methanococcus voltae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | 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 | Methanococcus voltae |
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