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1wne

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Revision as of 16:01, 11 April 2018

Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA

Structural highlights

1wne is a 3 chain structure with sequence from Foot-and-mouth disease virus c-s8c1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1u09
Gene:	Viruses (Foot-and-mouth disease virus C-S8c1)
Activity:	RNA-directed RNA polymerase, with EC number 2.7.7.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N. Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA. J Biol Chem. 2004 Nov 5;279(45):47212-21. Epub 2004 Aug 3. PMID:15294895 doi:10.1074/jbc.M405465200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wne"

@@ Line 1: / Line 1: @@
 ==Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA==
 <StructureSection load='1wne' size='340' side='right' caption='[[1wne]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Viruses ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=244367 Foot-and-mouth disease virus C-S8c1])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wne OCA], [http://pdbe.org/1wne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wne RCSB], [http://www.ebi.ac.uk/pdbsum/1wne PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wne OCA], [http://pdbe.org/1wne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wne RCSB], [http://www.ebi.ac.uk/pdbsum/1wne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wne ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wn/1wne_consurf.spt"</scriptWhenChecked>
+    <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>

1wne

From Proteopedia

Revision as of 16:01, 11 April 2018

Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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