Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-UvrC interaction

A crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB') has been solved to 3.0 Angstrom resolution. The domain adopts a helix-loop-helix fold which is stabilised by the packing of hydrophobic side-chains between helices, From the UvrB' fold, a model for a domain of UvrC (UvrC') that has high sequence homology with UvrB' has been made. In the crystal, a dimerisation of UvrB' domains is seen involving specific hydrophobic and salt bridge interactions between residues in and close to the loop region of the domain. It is proposed that a homologous mode of interaction may occur between UvrB and UvrC. This interaction is likely to be flexible, potentially spanning > 50 Angstrom. (C) 2000 Federation of European Biochemical Societies.