1cy1

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[[Image:1cy1.png|left|200px]]
 
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==COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPT==
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The line below this paragraph, containing "STRUCTURE_1cy1", creates the "Structure Box" on the page.
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<StructureSection load='1cy1' size='340' side='right'caption='[[1cy1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1cy1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CY1 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">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=THP:THYMIDINE-3,5-DIPHOSPHATE'>THP</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
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{{STRUCTURE_1cy1| PDB=1cy1 | SCENE= }}
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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=1cy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cy1 OCA], [https://pdbe.org/1cy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cy1 RCSB], [https://www.ebi.ac.uk/pdbsum/1cy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cy1 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/cy/1cy1_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=1cy1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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DNA topoisomerases are the enzymes responsible for controlling and maintaining the topological states of DNA. Type IA enzymes work by transiently breaking the phosphodiester backbone of one strand to allow passage of another strand through the break. The protein has to perform complex rearrangements of the DNA, and hence it is likely that different regions of the enzyme bind DNA with different affinities. In order to identify some of the DNA binding sites in the protein, we have solved the structures of several complexes of the 67 kDa N-terminal fragment of Escherichia coli DNA topoisomerase I with mono- and trinucleotides. There are five different binding sites in the complexes, one of which is adjacent to the active site. Two other sites are in the central hole of the protein and may represent general DNA binding regions. The positions of these sites allow us to identify different DNA binding regions and to understand their possible roles in the catalytic cycle.
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===COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPT===
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Protein-nucleotide interactions in E. coli DNA topoisomerase I.,Feinberg H, Changela A, Mondragon A Nat Struct Biol. 1999 Oct;6(10):961-8. PMID:10504732<ref>PMID:10504732</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_10504732}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1cy1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10504732 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10504732}}
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==About this Structure==
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[[1cy1]] is a 1 chain structure of [[Topoisomerase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CY1 OCA].
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==See Also==
==See Also==
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*[[Topoisomerase]]
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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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<ref group="xtra">PMID:10504732</ref><references group="xtra"/>
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__TOC__
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[[Category: DNA topoisomerase]]
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</StructureSection>
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[[Category: Escherichia coli k12]]
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[[Category: Escherichia coli K-12]]
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[[Category: Changela, A.]]
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[[Category: Large Structures]]
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[[Category: Feinberg, H.]]
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[[Category: Changela A]]
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[[Category: Mondragon, A.]]
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[[Category: Feinberg H]]
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[[Category: Dna topoisomerase]]
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[[Category: Mondragon A]]
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[[Category: Relaxing enzyme]]
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Current revision

COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPT

PDB ID 1cy1

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