The 55 residue C-terminal domain of UvrB that interacts with UvrC during excision repair in Escherichia coli has been expressed and purified as a (His)6 fusion construct. The fragment forms a stable folded domain in solution. Heteronuclear NMR experiments were used to obtain extensive 15N, 13C and 1H NMR assignments. NOESY and chemical shift data showed that the protein comprises two helices from residues 630 to 648 and from 652 to 670. 15N relaxation data also show that the first 11 and last three residues are unstructured. The effective rotational correlation time within the structured region is not consistent with a monomer. This oligomerisation may be relevant to the mode of dimerisation of UvrB with the homologous domain of UvrC. Copyright (C) 1999 Federation of European Biochemical Societies.
|Number of pages||5|
|State||Published - May 21 1999|
Bibliographical noteFunding Information:
This work was supported by the MRC and an EU Structural Biology Framework IV Programme grant. NMR spectra were recorded at the MRC Biomedical NMR Centre, Mill Hill. We are grateful to Dr. T. A. Frenkiel for assistance with NMR experiments, and Dr. J. Saldanha for analysing sequence alignments.
- Protein structure
- UvrB protein
- UvrC binding
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
- Cell Biology