2h7f: Difference between revisions

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-{{Seed}}
-[[Image:2h7f.png|left|200px]]
-<!--
+==Structure of variola topoisomerase covalently bound to DNA==
-The line below this paragraph, containing "STRUCTURE_2h7f", creates the "Structure Box" on the page.
+<StructureSection load='2h7f' size='340' side='right'caption='[[2h7f]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2h7f]] 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=2H7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H7F FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
-{{STRUCTURE_2h7f|  PDB=2h7f  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h7f OCA], [https://pdbe.org/2h7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h7f RCSB], [https://www.ebi.ac.uk/pdbsum/2h7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h7f ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h7/2h7f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2h7f ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Structure of variola topoisomerase covalently bound to DNA===
+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:16885024<ref>PMID:16885024</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2h7f" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16885024}}, adds the Publication Abstract to the page
+*[[Topoisomerase|Topoisomerase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16885024 is the PubMed ID number.
+*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_16885024}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-H7F is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Variola_virus Variola virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7F OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:16885024</ref><references group="xtra"/>
-[[Category: DNA topoisomerase]]
 [[Category: Variola virus]]
-[[Category: Bushman, F D.]]
+[[Category: Bushman FD]]
-[[Category: Duyne, G D.Van.]]
+[[Category: Hwang Y]]
-[[Category: Hwang, Y.]]
+[[Category: Perry K]]
-[[Category: Perry, K.]]
+[[Category: Van Duyne GD]]
-[[Category: Dna binding]]
-[[Category: Isomerase]]
-[[Category: Protein-dna complex]]
-[[Category: Type ib topoisomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:30:35 2009''