NMR assignments and secondary structure of the UvrC binding domain of UvrB.
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.
Alexandrovich
A
A
The Randall Institute, King's College, London, UK.
Sanderson
M R
MR
Moolenaar
G F
GF
Goosen
N
N
Lane
A N
AN
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D004265:DNA Helicases; D004706:Endodeoxyribonucleases; D004926:Escherichia coli / Q000737:chemistry; D029968:Escherichia coli Proteins; D009682:Magnetic Resonance Spectroscopy; D008954:Models, Biological; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D011993:Recombinant Fusion Proteins; C058093:UvrB protein, E coli; D004706:Endodeoxyribonucleases; C066567:UvrC protein, E coli; D004265:DNA Helicases