1n03
From Proteopedia
(New page: 200px<br /><applet load="1n03" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n03" /> '''Model for Active RecA Filament'''<br /> ==O...) |
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| - | [[Image:1n03.gif|left|200px]]<br /><applet load="1n03" size=" | + | [[Image:1n03.gif|left|200px]]<br /><applet load="1n03" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n03" /> | caption="1n03" /> | ||
'''Model for Active RecA Filament'''<br /> | '''Model for Active RecA Filament'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the E. coli RecA protein was solved more than 10 | + | The crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it has provided limited insight into the mechanism of homologous genetic recombination. Using electron microscopy, we have reconstructed five different states of RecA-DNA filaments. The C-terminal lobe of the RecA protein is modulated by the state of the distantly bound nucleotide, and this allosteric coupling can explain how mutations and truncations of this C-terminal lobe enhance RecA's activity. A model generated from these reconstructions shows that the nucleotide binding core is substantially rotated from its position in the RecA crystal filament, resulting in ATP binding between subunits. This simple rotation can explain the large cooperativity in ATP hydrolysis observed for RecA-DNA filaments. |
==About this Structure== | ==About this Structure== | ||
| - | 1N03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1N03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N03 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Campbell, M | + | [[Category: Campbell, M J.]] |
| - | [[Category: Egelman, E | + | [[Category: Egelman, E H.]] |
| - | [[Category: Lai, A | + | [[Category: Lai, A L.]] |
[[Category: Low, C.]] | [[Category: Low, C.]] | ||
| - | [[Category: VanLoock, M | + | [[Category: VanLoock, M S.]] |
[[Category: Yang, S.]] | [[Category: Yang, S.]] | ||
[[Category: Yu, X.]] | [[Category: Yu, X.]] | ||
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[[Category: helical polymer]] | [[Category: helical polymer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:46 2008'' |
Revision as of 12:00, 21 February 2008
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Model for Active RecA Filament
Overview
The crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it has provided limited insight into the mechanism of homologous genetic recombination. Using electron microscopy, we have reconstructed five different states of RecA-DNA filaments. The C-terminal lobe of the RecA protein is modulated by the state of the distantly bound nucleotide, and this allosteric coupling can explain how mutations and truncations of this C-terminal lobe enhance RecA's activity. A model generated from these reconstructions shows that the nucleotide binding core is substantially rotated from its position in the RecA crystal filament, resulting in ATP binding between subunits. This simple rotation can explain the large cooperativity in ATP hydrolysis observed for RecA-DNA filaments.
About this Structure
1N03 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
ATP-mediated conformational changes in the RecA filament., VanLoock MS, Yu X, Yang S, Lai AL, Low C, Campbell MJ, Egelman EH, Structure. 2003 Feb;11(2):187-96. PMID:12575938
Page seeded by OCA on Thu Feb 21 14:00:46 2008
