1v5w
From Proteopedia
(New page: 200px<br /> <applet load="1v5w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v5w, resolution 3.2Å" /> '''Crystal structure of...) |
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| - | [[Image:1v5w.gif|left|200px]]<br /> | + | [[Image:1v5w.gif|left|200px]]<br /><applet load="1v5w" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1v5w, resolution 3.2Å" /> | caption="1v5w, resolution 3.2Å" /> | ||
'''Crystal structure of the human Dmc1 protein'''<br /> | '''Crystal structure of the human Dmc1 protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human Dmc1 protein, a RecA/Rad51 homolog, is a meiosis-specific DNA | + | 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== | ==About this Structure== | ||
| - | 1V5W 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:// | + | 1V5W 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=1V5W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kinebuchi, T.]] | [[Category: Kinebuchi, T.]] | ||
[[Category: Kurumizaka, H.]] | [[Category: Kurumizaka, H.]] | ||
| - | [[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 15:31:55 2008'' |
Revision as of 13:31, 21 February 2008
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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 Thu Feb 21 15:31:55 2008
Categories: Homo sapiens | Single protein | Enomoto, R. | Ikawa, S. | Kagawa, W. | Kinebuchi, T. | Kurumizaka, H. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shibata, T. | Yokoyama, S. | Aaa atpase | Dna-binding protein | Octamer | Riken structural genomics/proteomics initiative | Ring protein | Rsgi | Structural genomics
