1kn0
From Proteopedia
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- | [[Image:1kn0.gif|left|200px]] | + | [[Image:1kn0.gif|left|200px]] |
- | + | ||
- | '''Crystal Structure of the human Rad52 protein''' | + | {{Structure |
+ | |PDB= 1kn0 |SIZE=350|CAPTION= <scene name='initialview01'>1kn0</scene>, resolution 2.85Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= Rad52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of the human Rad52 protein''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1KN0 is a [ | + | 1KN0 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=1KN0 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12191481 12191481] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ring protein]] | [[Category: ring protein]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
- | [[Category: structural | + | [[Category: structural genomic]] |
- | ''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 12:19:34 2008'' |
Revision as of 10:19, 20 March 2008
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, resolution 2.85Å | |||||||
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Gene: | Rad52 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 12:19:34 2008
Categories: Homo sapiens | Single protein | Fukai, S. | Ishitani, R. | Kagawa, W. | Kurumizaka, H. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shibata, T. | Yokoyama, S. | Beta-beta-beta-alpha fold | Dna-binding protein | Riken structural genomics/proteomics initiative | Ring protein | Rsgi | Structural genomic