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TitleATP-mediated conformational changes in the RecA filament.
Journal, issue, pagesStructure, Vol. 11, Issue 2, Page 187-196, Year 2003
Publish dateAug 27, 2003
AuthorsMargaret S VanLoock / Xiong Yu / Shixin Yang / Alex L Lai / Claudia Low / Michael J Campbell / Edward H Egelman /
PubMed AbstractThe 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 ...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.
External linksStructure / PubMed:12575938
MethodsEM (helical sym.)
Resolution20 Å
Structure data

PDB-1n03:
Model for Active RecA Filament
Method: ELECTRON MICROSCOPY / Resolution: 20.0 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • escherichia coli (E. coli)
KeywordsDNA BINDING PROTEIN / helical polymer

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