1yua

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(New page: 200px<br /><applet load="1yua" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yua" /> '''C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOIS...)
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'''C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I'''<br />
'''C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I'''<br />
==Overview==
==Overview==
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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 1H, 13C, and 15N, 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 +/- 0.11 A for the backbone atoms and 1.09 +/-, 0.09 A 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.
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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 1H, 13C, and 15N 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 +/- 0.11 A for the backbone atoms and 1.09 +/- 0.09 A 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.
==About this Structure==
==About this Structure==
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1YUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YUA OCA].
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1YUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUA OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fesik, S.W.]]
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[[Category: Fesik, S W.]]
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[[Category: Tse-Dinh, Y.C.]]
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[[Category: Tse-Dinh, Y C.]]
[[Category: Yu, L.]]
[[Category: Yu, L.]]
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[[Category: Zhu, C.X.]]
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[[Category: Zhu, C X.]]
[[Category: gene-regulating protein]]
[[Category: gene-regulating protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:10 2008''

Revision as of 14:09, 21 February 2008


1yua

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C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I

Overview

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 1H, 13C, and 15N 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 +/- 0.11 A for the backbone atoms and 1.09 +/- 0.09 A 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.

About this Structure

1YUA is a Single protein structure of sequence from Escherichia coli. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.

Reference

Solution structure of the C-terminal single-stranded DNA-binding domain of Escherichia coli topoisomerase I., Yu L, Zhu CX, Tse-Dinh YC, Fesik SW, Biochemistry. 1995 Jun 13;34(23):7622-8. PMID:7779808

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