1H2I

Human Rad52 protein, N-terminal domain

Summary for 1H2I

• Entry DOI: 10.2210/pdb1h2i/pdb
• Descriptor: DNA REPAIR PROTEIN RAD52 HOMOLOG (2 entities in total)
• Functional Keywords: dna-binding protein, dna repair, dna recombination, dna binding protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus : P43351
• Total number of polymer chains: 22
• Total formula weight: 507960.11

Authors

Singleton, M.R.,Wentzell, L.M.,Liu, Y.,West, S.C.,Wigley, D.B. (deposition date: 2002-08-09, release date: 2002-10-10, Last modification date: 2024-05-08)

Primary citation

Singleton, M.R.,Wentzell, L.M.,Liu, Y.,West, S.C.,Wigley, D.B.
Structure of the Single-Strand Annealing Domain of Human Rad52 Protein
Proc.Natl.Acad.Sci.USA, 99:13492-, 2002

PubMed 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.

PubMed: 12370410
DOI: 10.1073/PNAS.212449899

Experimental method

X-RAY DIFFRACTION (2.7 Å)