1wne: Difference between revisions

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-{{Seed}}
-[[Image:1wne.png|left|200px]]
-<!--
+==Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA==
-The line below this paragraph, containing "STRUCTURE_1wne", creates the "Structure Box" on the page.
+<StructureSection load='1wne' size='340' side='right'caption='[[1wne]], [[Resolution|resolution]] 3.00&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'>[[1wne]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus_C-S8c1 Foot-and-mouth disease virus C-S8c1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WNE 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]] 3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_1wne|  PDB=1wne  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wne OCA], [https://pdbe.org/1wne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wne RCSB], [https://www.ebi.ac.uk/pdbsum/1wne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wne ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9QCE4_9PICO Q9QCE4_9PICO] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266]  RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]
+== 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/wn/1wne_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1wne ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Genome replication in picornaviruses is catalyzed by a virally encoded RNA-dependent RNA polymerase, termed 3D. The enzyme performs this operation, together with other viral and probably host proteins, in the cytoplasm of their host cells. The crystal structure of the 3D polymerase of foot-and-mouth disease virus, one of the most important animal pathogens, has been determined unliganded and bound to a template-primer RNA decanucleotide. The enzyme folds in the characteristic fingers, palm and thumb subdomains, with the presence of an NH2-terminal segment that encircles the active site. In the complex, several conserved amino acid side chains bind to the template-primer, likely mediating the initiation of RNA synthesis. The structure provides essential information for studies on RNA replication and the design of antiviral compounds.
-===Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA===
+Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA.,Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N J Biol Chem. 2004 Nov 5;279(45):47212-21. Epub 2004 Aug 3. PMID:15294895<ref>PMID:15294895</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1wne" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15294895}}, adds the Publication Abstract to the page
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15294895 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15294895}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Foot-and-mouth disease virus C-S8c1]]
-WNE is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Foot_and_mouth_disease_virus Foot and mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNE OCA].
+[[Category: Large Structures]]
+[[Category: Arias A]]
-==Reference==
+[[Category: Domingo E]]
-<ref group="xtra">PMID:15294895</ref><references group="xtra"/>
+[[Category: Escarmis C]]
-[[Category: Foot and mouth disease virus]]
+[[Category: Ferrer-Orta C]]
-[[Category: RNA-directed RNA polymerase]]
+[[Category: Perez-Luque R]]
-[[Category: Arias, A.]]
+[[Category: Verdaguer N]]
-[[Category: Domingo, E.]]
-[[Category: Escarmis, C.]]
-[[Category: Ferrer-Orta, C.]]
-[[Category: Perez-Luque, R.]]
-[[Category: Verdaguer, N.]]
-[[Category: Foot and mouth disease virus]]
-[[Category: Protein-dna complex]]
-[[Category: Rna-dependent rna polymerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:51:32 2009''