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 (RAD521-212) forms an undecameric ring structure with a surface that is mostly positively charged. In the present study, it was found that RAD521-212 containing alanine mutations of the charged surface residues (Lys102, Lys133 and Glu202) is highly amenable to crystallization. The structure of the mutant RAD521-212 was solved at 2.4 Å resolution. The structure revealed an association between the symmetry-related RAD521-212 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 RAD521-212 ring and stabilized the ring-ring association observed in the crystal.
|ジャーナル||Acta Crystallographica Section F:Structural Biology Communications|
|出版ステータス||Published - 2016|
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