1N03

Model for Active RecA Filament

Summary for 1N03

• Entry DOI: 10.2210/pdb1n03/pdb
• Descriptor: RecA protein, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: helical polymer, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 7
• Total formula weight: 268186.01

Authors

VanLoock, M.S.,Yu, X.,Yang, S.,Lai, A.L.,Low, C.,Campbell, M.J.,Egelman, E.H. (deposition date: 2002-10-10, release date: 2003-02-25, Last modification date: 2024-02-14)

Primary citation

VanLoock, M.S.,Yu, X.,Yang, S.,Lai, A.L.,Low, C.,Campbell, M.J.,Egelman, E.H.
ATP-Mediated Conformational Changes in the RecA Filament
Structure, 11:187-196, 2003

PubMed Abstract: 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.

PubMed: 12575938
DOI: 10.1016/S0969-2126(03)00003-0

Experimental method

ELECTRON MICROSCOPY (20 Å)