1aa3

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C-TERMINAL DOMAIN OF THE E. COLI RECA, NMR, MINIMIZED AVERAGE STRUCTURE

Overview

RecA protein and its homologs catalyze homologous pairing of dsDNA and, ssDNA, a critical reaction in homologous genetic recombination in various, organisms from a virus, microbes to higher eukaryotes. In this reaction, RecA protein forms a nucleoprotein filament on ssDNA, which in turn binds, to naked dsDNA for homology search. We suggested that the C-terminal, domain of RecA protein plays a role in capturing the dsDNA. Here, we, isolated the C-terminal domain as a soluble form and determined the, solution structure by NMR spectroscopy. The overall folding of the NMR, structure agrees with that of the corresponding part of the reported, crystal structure, but a remarkable difference was found in a, solvent-exposed region due to intermolecular contacts in the crystal., Then, we studied the interaction between the C-terminal domain and DNA, and found that significant chemical shift changes were induced in a, specific region by titration with dsDNA. SsDNA induced a much smaller, chemical shift perturbation. The difference of DNA concentrations to give, the half-saturation of the chemical shift change showed a higher affinity, of the C-terminal region toward dsDNA. Combined with our previous results, these provide direct evidence that the defined region in the C-terminal, domain furnishes a binding surface for DNA.

About this Structure

1AA3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing., Aihara H, Ito Y, Kurumizaka H, Terada T, Yokoyama S, Shibata T, J Mol Biol. 1997 Nov 28;274(2):213-21. PMID:9398528

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