NDLI: Structure of the single-strand annealing domain of human RAD52 protein.

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Structure of the single-strand annealing domain of human RAD52 protein.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wentzell, Lois M. Liu, Yilun Singleton, Martin R. Wigley, Dale B. West, Stephen C.
Description	Author Affiliation: Singleton MR ( Cancer Research U.K., London Research Institute, Clare Hall Laboratories, South Mimms, Hertfordshire EN6 3LD, UK.);
Abstract	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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA-Binding Proteins Chemistry Binding Sites Crystallography, X-Ray DNA Repair DNA, Single-Stranded Metabolism Genetics Models, Molecular Molecular Structure Peptide Fragments Protein Folding Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Rad52 DNA Repair And Recombination Protein Recombinant Proteins Static Electricity Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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