1KN0

Crystal Structure of the human Rad52 protein

1KN0 の概要

• エントリーDOI: 10.2210/pdb1kn0/pdb
• 分子名称: Rad52 (2 entities in total)
• 機能のキーワード: beta-beta-beta-alpha fold, dna-binding protein, ring protein, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (Potential): P43351
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 257746.61

構造登録者

Kagawa, W.,Kurumizaka, H.,Ishitani, R.,Fukai, S.,Nureki, O.,Shibata, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2001-12-18, 公開日: 2002-09-04, 最終更新日: 2024-03-13)

主引用文献

Kagawa, W.,Kurumizaka, H.,Ishitani, R.,Fukai, S.,Nureki, O.,Shibata, T.,Yokoyama, S.
Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form.
Mol.Cell, 10:359-371, 2002

PubMed Abstract: The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.

PubMed: 12191481
DOI: 10.1016/S1097-2765(02)00587-7

実験手法

X-RAY DIFFRACTION (2.85 Å)