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Published on: December 21, 2010
Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction
M Sohi1, A Alexandrovich, G Moolenaar
1The Randall Institute, King's College, 26-29 Drury Lane, London, UK.
Abstract:
A crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB') has been solved to 3.0 A 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 A.
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