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NMR assignments and secondary structure of the UvrC binding domain of UvrB
Author(s) -
Alexandrovich Alexander,
Sanderson Mark R.,
Moolenaar Geri F.,
Goosen Nora,
Lane Andrew N.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00542-6
Subject(s) - heteronuclear molecule , chemistry , two dimensional nuclear magnetic resonance spectroscopy , monomer , crystallography , stereochemistry , nuclear magnetic resonance spectroscopy , organic chemistry , polymer
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 15 N, 13 C and 1 H NMR assignments. NOESY and chemical shift data showed that the protein comprises two helices from residues 630 to 648 and from 652 to 670. 15 N 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.