1h2i
From Proteopedia
(New page: 200px<br /> <applet load="1h2i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h2i, resolution 2.7Å" /> '''HUMAN RAD52 PROTEIN,...) |
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| - | [[Image:1h2i.gif|left|200px]]<br /> | + | [[Image:1h2i.gif|left|200px]]<br /><applet load="1h2i" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h2i" size=" | + | |
caption="1h2i, resolution 2.7Å" /> | caption="1h2i, resolution 2.7Å" /> | ||
'''HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN'''<br /> | '''HUMAN RAD52 PROTEIN, N-TERMINAL DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In eukaryotic cells, RAD52 protein plays a central role in genetic | + | 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== | ==About this Structure== | ||
| - | 1H2I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1H2I is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
| - | [[Category: Singleton, M | + | [[Category: Singleton, M R.]] |
| - | [[Category: Wentzell, L | + | [[Category: Wentzell, L M.]] |
| - | [[Category: West, S | + | [[Category: West, S C.]] |
| - | [[Category: Wigley, D | + | [[Category: Wigley, D B.]] |
[[Category: dna recombination]] | [[Category: dna recombination]] | ||
[[Category: dna repair]] | [[Category: dna repair]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:37 2008'' |
Revision as of 10:56, 21 February 2008
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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 Thu Feb 21 12:56:37 2008
