1kn0
From Proteopedia
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Crystal Structure of the human Rad52 protein
Overview
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.
About this Structure
1KN0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form., Kagawa W, Kurumizaka H, Ishitani R, Fukai S, Nureki O, Shibata T, Yokoyama S, Mol Cell. 2002 Aug;10(2):359-71. PMID:12191481
Page seeded by OCA on Mon Nov 12 17:52:46 2007
Categories: Homo sapiens | Single protein | Fukai, S. | Ishitani, R. | Kagawa, W. | Kurumizaka, H. | Nureki, O. | RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative. | Shibata, T. | Yokoyama, S. | Beta-beta-beta-alpha fold | Dna-binding protein | Riken structural genomics/proteomics initiative | Ring protein | Rsgi | Structural genomics
