1n03
From Proteopedia
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 Sat May 3 01:55:21 2008
