2d7s
From Proteopedia
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| - | [[Image:2d7s.png|left|200px]] | ||
| - | + | ==Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with VPg protein== | |
| + | <StructureSection load='2d7s' size='340' side='right'caption='[[2d7s]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2d7s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Foot_and_mouth_disease_virus_C Foot and mouth disease virus C] and [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=2D7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D7S FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7s OCA], [https://pdbe.org/2d7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d7s RCSB], [https://www.ebi.ac.uk/pdbsum/2d7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d7s 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/d7/2d7s_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=2d7s ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Picornavirus RNA replication is initiated by the covalent attachment of a UMP molecule to the hydroxyl group of a tyrosine in the terminal protein VPg. This reaction is carried out by the viral RNA-dependent RNA polymerase (3D). Here, we report the X-ray structure of two complexes between foot-and-mouth disease virus 3D, VPg1, the substrate UTP and divalent cations, in the absence and in the presence of an oligoadenylate of 10 residues. In both complexes, VPg fits the RNA binding cleft of the polymerase and projects the key residue Tyr3 into the active site of 3D. This is achieved by multiple interactions with residues of motif F and helix alpha8 of the fingers domain and helix alpha13 of the thumb domain of the polymerase. The complex obtained in the presence of the oligoadenylate showed the product of the VPg uridylylation (VPg-UMP). Two metal ions and the catalytic aspartic acids of the polymerase active site, together with the basic residues of motif F, have been identified as participating in the priming reaction. | ||
| - | + | The structure of a protein primer-polymerase complex in the initiation of genome replication.,Ferrer-Orta C, Arias A, Agudo R, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N EMBO J. 2006 Feb 22;25(4):880-8. Epub 2006 Feb 2. PMID:16456546<ref>PMID:16456546</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2d7s" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[RNA polymerase|RNA polymerase]] | + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: Foot-and-mouth disease virus | + | </StructureSection> |
| - | [[Category: | + | [[Category: Foot and mouth disease virus C]] |
| - | [[Category: Arias | + | [[Category: Foot-and-mouth disease virus C-S8c1]] |
| - | [[Category: Domingo | + | [[Category: Large Structures]] |
| - | [[Category: Escarmis | + | [[Category: Arias A]] |
| - | [[Category: Ferrer-Orta | + | [[Category: Domingo E]] |
| - | [[Category: Perez-Luque | + | [[Category: Escarmis C]] |
| - | [[Category: Verdaguer | + | [[Category: Ferrer-Orta C]] |
| - | + | [[Category: Perez-Luque R]] | |
| - | + | [[Category: Verdaguer N]] | |
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Current revision
Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with VPg protein
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