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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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[[Image:1yua.gif|left|200px]]<br /><applet load="1yua" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yua" />
 
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'''C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I'''<br />
 
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==Overview==
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==C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I==
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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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<StructureSection load='1yua' size='340' side='right'caption='[[1yua]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yua]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YUA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yua OCA], [https://pdbe.org/1yua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yua RCSB], [https://www.ebi.ac.uk/pdbsum/1yua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yua ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TOP1_ECOLI TOP1_ECOLI] Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.<ref>PMID:9497321</ref> <ref>PMID:10681504</ref> <ref>PMID:21482796</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yu/1yua_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yua ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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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*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
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== References ==
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==Reference==
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<references/>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7779808 7779808]
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__TOC__
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[[Category: DNA topoisomerase]]
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fesik, S.W.]]
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[[Category: Fesik SW]]
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[[Category: Tse-Dinh, Y.C.]]
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[[Category: Tse-Dinh Y-C]]
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[[Category: Yu, L.]]
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[[Category: Yu L]]
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[[Category: Zhu, C.X.]]
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[[Category: Zhu C-X]]
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[[Category: gene-regulating protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:03:19 2007''
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C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I

PDB ID 1yua

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