1h2i: Difference between revisions
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'''HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN''' | {{Structure | ||
|PDB= 1h2i |SIZE=350|CAPTION= <scene name='initialview01'>1h2i</scene>, resolution 2.7Å | |||
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|LIGAND= | |||
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'''HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1H2I is a [ | 1H2I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2I OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12370410 12370410] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:31:15 2008'' | ||
Revision as of 09:31, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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