1n03
From Proteopedia
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| - | [[Image:1n03.gif|left|200px]] | + | [[Image:1n03.gif|left|200px]] |
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| - | '''Model for Active RecA Filament''' | + | {{Structure |
| + | |PDB= 1n03 |SIZE=350|CAPTION= <scene name='initialview01'>1n03</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Model for Active RecA Filament''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N03 is a [ | + | 1N03 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N03 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12575938 12575938] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helical polymer]] | [[Category: helical polymer]] | ||
| - | ''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 12:50:22 2008'' |
Revision as of 10:50, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 12:50:22 2008
