1kn0

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[[Image:1kn0.gif|left|200px]]
[[Image:1kn0.gif|left|200px]]
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{{Structure
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|PDB= 1kn0 |SIZE=350|CAPTION= <scene name='initialview01'>1kn0</scene>, resolution 2.85&Aring;
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The line below this paragraph, containing "STRUCTURE_1kn0", creates the "Structure Box" on the page.
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|SITE=
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|GENE= Rad52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1kn0| PDB=1kn0 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn0 OCA], [http://www.ebi.ac.uk/pdbsum/1kn0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kn0 RCSB]</span>
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'''Crystal Structure of the human Rad52 protein'''
'''Crystal Structure of the human Rad52 protein'''
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[[Category: Shibata, T.]]
[[Category: Shibata, T.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: beta-beta-beta-alpha fold]]
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[[Category: Beta-beta-beta-alpha fold]]
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[[Category: dna-binding protein]]
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[[Category: Dna-binding protein]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: ring protein]]
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[[Category: Ring protein]]
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[[Category: rsgi]]
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[[Category: Rsgi]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:49 2008''
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Revision as of 19:56, 2 May 2008

Template:STRUCTURE 1kn0

Crystal Structure of the human Rad52 protein


Overview

The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.

About this Structure

1KN0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form., Kagawa W, Kurumizaka H, Ishitani R, Fukai S, Nureki O, Shibata T, Yokoyama S, Mol Cell. 2002 Aug;10(2):359-71. PMID:12191481 Page seeded by OCA on Fri May 2 22:56:01 2008

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