1kn0: Difference between revisions
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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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| 1kn0, 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
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
