5JRB

Rad52(1-212) K102A/K133A/E202A mutant

5JRB の概要

• エントリーDOI: 10.2210/pdb5jrb/pdb
• 分子名称: DNA repair protein RAD52 homolog (2 entities in total)
• 機能のキーワード: dna annealing protein, ssdna binding, multimeric ring formation, dna binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 258935.02

構造登録者

Saotome, M.,Saito, K.,Kurumizaka, H.,Kagawa, W. (登録日: 2016-05-06, 公開日: 2016-08-10, 最終更新日: 2023-11-08)

主引用文献

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

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: 27487923
DOI: 10.1107/S2053230X1601027X

実験手法

X-RAY DIFFRACTION (2.405 Å)