5JRB
Rad52(1-212) K102A/K133A/E202A mutant
Summary for 5JRB
| Entry DOI | 10.2210/pdb5jrb/pdb |
| Descriptor | DNA repair protein RAD52 homolog (2 entities in total) |
| Functional Keywords | dna annealing protein, ssdna binding, multimeric ring formation, dna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 11 |
| Total formula weight | 258935.02 |
| Authors | Saotome, M.,Saito, K.,Kurumizaka, H.,Kagawa, W. (deposition date: 2016-05-06, release date: 2016-08-10, Last modification date: 2023-11-08) |
| Primary citation | Saotome, M.,Saito, K.,Onodera, K.,Kurumizaka, H.,Kagawa, W. Structure of the human DNA-repair protein RAD52 containing surface mutations. Acta Crystallogr.,Sect.F, 72:598-603, 2016 Cited by PubMed Abstract: The Rad52 protein is a eukaryotic single-strand DNA-annealing protein that is involved in the homologous recombinational repair of DNA double-strand breaks. The isolated N-terminal half of the human RAD52 protein (RAD52(1-212)) forms an undecameric ring structure with a surface that is mostly positively charged. In the present study, it was found that RAD52(1-212) containing alanine mutations of the charged surface residues (Lys102, Lys133 and Glu202) is highly amenable to crystallization. The structure of the mutant RAD52(1-212) was solved at 2.4 Å resolution. The structure revealed an association between the symmetry-related RAD52(1-212) rings, in which a partially unfolded, C-terminal region of RAD52 extended into the DNA-binding groove of the neighbouring ring in the crystal. The alanine mutations probably reduced the surface entropy of the RAD52(1-212) ring and stabilized the ring-ring association observed in the crystal. PubMed: 27487923DOI: 10.1107/S2053230X1601027X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.405 Å) |
Structure validation
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