1v5w

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[[Image:1v5w.gif|left|200px]]
[[Image:1v5w.gif|left|200px]]
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{{Structure
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|PDB= 1v5w |SIZE=350|CAPTION= <scene name='initialview01'>1v5w</scene>, resolution 3.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1v5w", creates the "Structure Box" on the page.
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|GENE= DMC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1v5w| PDB=1v5w | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5w OCA], [http://www.ebi.ac.uk/pdbsum/1v5w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v5w RCSB]</span>
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'''Crystal structure of the human Dmc1 protein'''
'''Crystal structure of the human Dmc1 protein'''
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[[Category: Shibata, T.]]
[[Category: Shibata, T.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: aaa atpase]]
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[[Category: Aaa atpase]]
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[[Category: dna-binding protein]]
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[[Category: Dna-binding protein]]
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[[Category: octamer]]
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[[Category: Octamer]]
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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 Sat May 3 12:07:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:19:52 2008''
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Revision as of 09:07, 3 May 2008

Template:STRUCTURE 1v5w

Crystal structure of the human Dmc1 protein


Overview

The human Dmc1 protein, a RecA/Rad51 homolog, is a meiosis-specific DNA recombinase that catalyzes homologous pairing. RecA and Rad51 form helical filaments, while Dmc1 forms an octameric ring. In the present study, we crystallized the full-length human Dmc1 protein and solved the structure of the Dmc1 octameric ring. The monomeric structure of the Dmc1 protein closely resembled those of the human and archaeal Rad51 proteins. In addition to the polymerization motif that was previously identified in the Rad51 proteins, we found another hydrogen bonding interaction at the polymer interface, which could explain why Dmc1 forms stable octameric rings instead of helical filaments. Mutagenesis studies identified the inner and outer basic patches that are important for homologous pairing. The inner patch binds both single-stranded and double-stranded DNAs, while the outer one binds single-stranded DNA. Based on these results, we propose a model for the interaction of the Dmc1 rings with DNA.

About this Structure

1V5W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1., Kinebuchi T, Kagawa W, Enomoto R, Tanaka K, Miyagawa K, Shibata T, Kurumizaka H, Yokoyama S, Mol Cell. 2004 May 7;14(3):363-74. PMID:15125839 Page seeded by OCA on Sat May 3 12:07:15 2008

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