| Literature DB >> 12191481 |
Wataru Kagawa1, Hitoshi Kurumizaka, Ryuichiro Ishitani, Shuya Fukai, Osamu Nureki, Takehiko Shibata, Shigeyuki Yokoyama.
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.Entities:
Mesh：
Substances：
Year: 2002 PMID： 12191481 DOI： 10.1016/s1097-2765(02)00587-7
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970