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helix-hairpin-helix domain-containing protein
RuvA, C-terminal domain
Homologous recombination is a crucial process in all living organisms. In bacteria, this process the RuvA, RuvB, and RuvC proteins are involved. More specifically the proteins process the Holliday junction DNA. RuvA is comprised of three distinct domains. The domain represents the C-terminal domain and plays a significant role in the ATP-dependent branch migration of the hetero-duplex through direct contact with RuvB [1]. Within the Holliday junction, the C-terminal domain makes no interaction with DNA [1]. [1]. 10890893. Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer. Ariyoshi M, Nishino T, Iwasaki H, Shinagawa H, Morikawa K;. Proc Natl Acad Sci U S A 2000;97:8257-8262. (from Pfam)
OB-fold domain-containing protein
The N terminal domain of RuvA has an OB-fold structure. This domain forms the RuvA tetramer contacts [1]. [1]. 8832889. Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Rafferty JB, Sedelnikova SE, Hargreaves D, Artymiuk PJ, Baker PJ, Sharples GJ, Mahdi AA, Lloyd RG, Rice DW;. Science 1996;274:415-421. (from Pfam)
Holliday junction branch migration protein RuvA
RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions.
Holliday junction branch migration protein RuvA is an ATP-dependent DNA helicase involved in branch migration of heteroduplex DNA in homologous recombination, by stimulating the ATPase activity of RuvB
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