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==2.75 angstrom structure of the D347G D348G mutant structure of Sapporo Virus RdRp Polymerase== | ==2.75 angstrom structure of the D347G D348G mutant structure of Sapporo Virus RdRp Polymerase== | ||
<StructureSection load='2uuw' size='340' side='right' caption='[[2uuw]], [[Resolution|resolution]] 2.76Å' scene=''> | <StructureSection load='2uuw' size='340' side='right' caption='[[2uuw]], [[Resolution|resolution]] 2.76Å' scene=''> | ||
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ckw|2ckw]], [[2uut|2uut]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ckw|2ckw]], [[2uut|2uut]]</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='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=2uuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uuw OCA], [http://pdbe.org/2uuw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uuw RCSB], [http://www.ebi.ac.uk/pdbsum/2uuw 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=2uuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uuw OCA], [http://pdbe.org/2uuw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uuw RCSB], [http://www.ebi.ac.uk/pdbsum/2uuw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uuw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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=2uuw ConSurf]. | </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=2uuw ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 17:34, 15 November 2017
2.75 angstrom structure of the D347G D348G mutant structure of Sapporo Virus RdRp Polymerase2.75 angstrom structure of the D347G D348G mutant structure of Sapporo Virus RdRp Polymerase
Structural highlights
Function[POLG_SVM93] NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity (By similarity). Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation (By similarity). Protease-polymerase processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved (By similarity). Protease-polymerase is a RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Catalyzes the covalent attachment VPg with viral RNAs (By similarity). Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human calicivirus slv
- RNA-directed RNA polymerase
- Fullerton, S
- Gebhardt, J
- Robel, I
- Rohayem, J
- Schuldt, L
- Tucker, P
- Atp-binding
- Capsid protein
- Covalent protein-rna linkage
- Helicase
- Hydrolase
- Nucleotide-binding
- Nucleotidyltransferase
- Polyprotein
- Protease
- Rna elongation
- Rna replication
- Rna-directed rna polymerase
- Structural protein
- Thiol protease
- Transferase
- Transferase activity