7XHJ
Crystal structure of RuvC from Deinococcus radiodurans
Summary for 7XHJ
| Entry DOI | 10.2210/pdb7xhj/pdb |
| Descriptor | Crossover junction endodeoxyribonuclease RuvC (2 entities in total) |
| Functional Keywords | nuclease, dna repair, homologous recombination, holliday junction resolvase, dna binding protein |
| Biological source | Deinococcus radiodurans ATCC 13939 |
| Total number of polymer chains | 2 |
| Total formula weight | 39363.68 |
| Authors | |
| Primary citation | Qin, C.,Han, W.,Xu, Y.,Zhao, Y.,Xu, H.,Tian, B.,Wang, L.,Hua, Y. Structural and Functional Characterization of the Holliday Junction Resolvase RuvC from Deinococcus radiodurans. Microorganisms, 10:-, 2022 Cited by PubMed Abstract: Holliday junctions (HJs) are four-way DNA structures, which are an important intermediate in the process of homologous recombination. In most bacteria, HJs are cleaved by specific nucleases called RuvC resolvases at the end of homologous recombination. is an extraordinary radiation-resistant bacterium and is known as an ideal model organism for elucidating DNA repair processes. Here, we described the biochemical properties and the crystal structure of RuvC from (RuvC). RuvC exhibited an RNase H fold that belonged to the retroviral integrase family. Among many DNA substrates, RuvC specifically bound to HJ DNA and cleaved it. In particular, Mn was the preferred bivalent metal co-factor for HJ cleavage, whereas high concentrations of Mg inhibited the binding of RuvC to HJ. In addition, RuvC was crystallized and the crystals diffracted to 1.6 Å. The crystal structure of RuvC revealed essential amino acid sites for cleavage and binding activities, indicating that RuvC was a typical resolvase with a characteristic choice for metal co-factor. PubMed: 35744678DOI: 10.3390/microorganisms10061160 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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