Crystal structure of Escherichia coli UvrB C‐terminal domain, and a model for UvrB‐UvrC interaction
Open Access
- 14 January 2000
- journal article
- Published by Wiley in FEBS Letters
- Vol. 465 (2-3) , 161-164
- https://doi.org/10.1016/s0014-5793(99)01690-7
Abstract
A crystal structure of the C‐terminal domain of Escherichia coli UvrB (UvrB′) has been solved to 3.0 Å 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 Å.Keywords
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