Journal article
Solution structure of the C-terminal single-stranded DNA-binding domain of Escherichia coli topoisomerase I
Biochemistry (Easton), Vol.34(23), pp.7622-7628
06/1995
DOI: 10.1021/bi00023a008
PMID: 7779808
Abstract
Escherichia coli DNA topoisomerase I catalyzes the interconversion of different topological forms of DNA. In this paper we describe NMR studies of a 14K C-terminal fragment of this enzyme that binds preferentially to single-stranded DNA and enhances the enzyme's ability to relax negatively supercoiled DNA under high salt conditions. The super(1)H, super(13)C, and super(15)N resonances of the protein were assigned from a number of heteronuclear multidimensional NMR experiments, and the three-dimensional structure of the protein was determined from a total of 2188 NMR-derived restraints. The root-mean-square deviation about the mean coordinate positions for residues 13-120 is 0.68 plus or minus 0.11 angstrom for the backbone atoms and 1.09 plus or minus 0.09 angstrom for all heavy atoms. The overall fold, which consists of two four-stranded beta -sheets separated by two helices, differs from other DNA- and RNA-binding proteins such as gene 5, cold shock protein, and hnRNP C. From an analysis of the changes in chemical shift upon the addition of single-stranded DNA, the location of the oligonucleotide binding site was determined. The binding site consists of a beta -sheet containing positively charged and aromatic amino acids and, in spite of its different structure, is similar to that found in other proteins that bind single-stranded oligonucleotides.
Details
- Title: Subtitle
- Solution structure of the C-terminal single-stranded DNA-binding domain of Escherichia coli topoisomerase I
- Creators
- Liping YuChang-Xi ZhuYuk-Ching Tse-DinhS Fesik
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.34(23), pp.7622-7628
- DOI
- 10.1021/bi00023a008
- PMID
- 7779808
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 06/1995
- Academic Unit
- Biochemistry and Molecular Biology; Medicine Administration
- Record Identifier
- 9984627302302771
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