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Publication Abstract from PubMed

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 A 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.

Structure of the human DNA-repair protein RAD52 containing surface mutations.,Saotome M, Saito K, Onodera K, Kurumizaka H, Kagawa W Acta Crystallogr F Struct Biol Commun. 2016 Aug;72(Pt 8):598-603. doi:, 10.1107/S2053230X1601027X. Epub 2016 Jul 13. PMID:27487923^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.