1kn0
From Proteopedia
(New page: 200px<br /> <applet load="1kn0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kn0, resolution 2.85Å" /> '''Crystal Structure o...) |
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| - | [[Image:1kn0.gif|left|200px]]<br /> | + | [[Image:1kn0.gif|left|200px]]<br /><applet load="1kn0" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1kn0" size=" | + | |
caption="1kn0, resolution 2.85Å" /> | caption="1kn0, resolution 2.85Å" /> | ||
'''Crystal Structure of the human Rad52 protein'''<br /> | '''Crystal Structure of the human Rad52 protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human Rad52 protein forms a heptameric ring that catalyzes homologous | + | 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== | ==About this Structure== | ||
| - | 1KN0 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:// | + | 1KN0 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=1KN0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kurumizaka, H.]] | [[Category: Kurumizaka, H.]] | ||
[[Category: Nureki, O.]] | [[Category: Nureki, O.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shibata, T.]] | [[Category: Shibata, T.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:54 2008'' |
Revision as of 11:35, 21 February 2008
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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 Feb 21 13:35:54 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 genomics
