2h7g

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(New page: 200px<br /><applet load="2h7g" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h7g, resolution 1.900&Aring;" /> '''Structure of variol...)
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[[Image:2h7g.gif|left|200px]]<br /><applet load="2h7g" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h7g, resolution 1.900&Aring;" />
 
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'''Structure of variola topoisomerase non-covalently bound to DNA'''<br />
 
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==Overview==
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==Structure of variola topoisomerase non-covalently bound to DNA==
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Although smallpox has been eradicated from the human population, it is, presently feared as a possible agent of bioterrorism. The smallpox virus, codes for its own topoisomerase enzyme that differs from its cellular, counterpart by requiring a specific DNA sequence for activation of, catalysis. Here we present crystal structures of the smallpox virus, topoisomerase enzyme bound both covalently and noncovalently to a specific, DNA sequence. These structures reveal the basis for site-specific DNA, recognition, and they explain how catalysis is likely activated by, formation of a specific enzyme-DNA interface. Unexpectedly, the poxvirus, enzyme uses a major groove binding alpha helix that is not present in the, human enzyme to recognize part of the core recognition sequence and, activate the enzyme for catalysis. The topoisomerase-DNA complex, structures also provide a three-dimensional framework that may facilitate, the rational design of therapeutic agents to treat poxvirus infections.
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<StructureSection load='2h7g' size='340' side='right'caption='[[2h7g]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2h7g]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Variola_virus Variola virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H7G 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]] 1.9&#8491;</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=2h7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h7g OCA], [https://pdbe.org/2h7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h7g RCSB], [https://www.ebi.ac.uk/pdbsum/2h7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h7g ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TOP1_VAR67 TOP1_VAR67] Releases the supercoiling and torsional tension of DNA 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 the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-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 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
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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/h7/2h7g_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=2h7g 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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2H7G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Variola_virus Variola virus]. 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=2H7G OCA].
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*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis for specificity in the poxvirus topoisomerase., Perry K, Hwang Y, Bushman FD, Van Duyne GD, Mol Cell. 2006 Aug 4;23(3):343-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16885024 16885024]
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[[Category: Large Structures]]
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[[Category: DNA topoisomerase]]
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[[Category: Single protein]]
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[[Category: Variola virus]]
[[Category: Variola virus]]
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[[Category: Bushman, F.D.]]
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[[Category: Bushman FD]]
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[[Category: Duyne, G.D.Van.]]
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[[Category: Hwang Y]]
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[[Category: Hwang, Y.]]
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[[Category: Perry K]]
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[[Category: Perry, K.]]
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[[Category: Van Duyne GD]]
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[[Category: dna binding]]
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[[Category: isomerase]]
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[[Category: protein-dna complex]]
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[[Category: type ib topoisomerase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:35:09 2007''
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Current revision

Structure of variola topoisomerase non-covalently bound to DNA

PDB ID 2h7g

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