1h2i
From Proteopedia
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'''HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN''' | '''HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN''' | ||
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[[Category: West, S C.]] | [[Category: West, S C.]] | ||
[[Category: Wigley, D B.]] | [[Category: Wigley, D B.]] | ||
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Revision as of 15:20, 2 May 2008
HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN
Overview
In eukaryotic cells, RAD52 protein plays a central role in genetic recombination and DNA repair by (i) promoting the annealing of complementary single-stranded DNA and (ii) stimulation of the RAD51 recombinase. The single-strand annealing domain resides in the N-terminal region of the protein and is highly conserved, whereas the nonconserved RAD51-interaction domain is located in the C-terminal region. An N-terminal fragment of human RAD52 (residues 1-209) has been purified to homogeneity and, similar to the full-size protein (residues 1-418), shown to promote single-strand annealing in vitro. We have determined the crystal structure of this single-strand annealing domain at 2.7 A. The structure reveals an undecameric (11) subunit ring with extensive subunit contacts. A large, positively charged groove runs along the surface of the ring, readily suggesting a mechanism by which RAD52 presents the single strand for reannealing with complementary single-stranded DNA.
About this Structure
1H2I is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the single-strand annealing domain of human RAD52 protein., Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB, Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13492-7. Epub 2002 Oct 7. PMID:12370410 Page seeded by OCA on Fri May 2 18:20:32 2008
