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<StructureSection load='6rid' size='340' side='right'caption='[[6rid]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='6rid' size='340' side='right'caption='[[6rid]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6rid]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RID FirstGlance]. <br> | <table><tr><td colspan='2'>[[6rid]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus_glv-1h68 Vaccinia virus glv-1h68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RID FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rfg|6rfg]], [[6rfl|6rfl]], [[6rie|6rie]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rfg|6rfg]], [[6rfl|6rfl]], [[6rie|6rie]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GL125 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68]), GL194 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68]), GL205 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68]), GL123 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68]), GL167 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68]), GL147 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68]), GL107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68]), GL076 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502057 Vaccinia virus GLV-1h68])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </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=6rid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rid OCA], [http://pdbe.org/6rid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rid RCSB], [http://www.ebi.ac.uk/pdbsum/6rid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rid ProSAT]</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=6rid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rid OCA], [http://pdbe.org/6rid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rid RCSB], [http://www.ebi.ac.uk/pdbsum/6rid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rid ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/B9U1R2_9POXV B9U1R2_9POXV]] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000746] [[http://www.uniprot.org/uniprot/B9U1I0_9POXV B9U1I0_9POXV]] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000744] [[http://www.uniprot.org/uniprot/B9U1M4_9POXV B9U1M4_9POXV]] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000743] | [[http://www.uniprot.org/uniprot/B9U1R2_9POXV B9U1R2_9POXV]] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000746] [[http://www.uniprot.org/uniprot/B9U1I0_9POXV B9U1I0_9POXV]] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000744] [[http://www.uniprot.org/uniprot/B9U1M4_9POXV B9U1M4_9POXV]] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000743] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Poxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate m(7)G-capped mRNAs in the host cytoplasm. In the accompanying paper, we report structures of core and complete vRNAP complexes of the prototypic Vaccinia poxvirus (Grimm et al., 2019; in this issue of Cell). Here, we present the cryo-electron microscopy (cryo-EM) structures of Vaccinia vRNAP in the form of a transcribing elongation complex and in the form of a co-transcriptional capping complex that contains the viral capping enzyme (CE). The trifunctional CE forms two mobile modules that bind the polymerase surface around the RNA exit tunnel. RNA extends from the vRNAP active site through this tunnel and into the active site of the CE triphosphatase. Structural comparisons suggest that growing RNA triggers large-scale rearrangements on the surface of the transcription machinery during the transition from transcription initiation to RNA capping and elongation. Our structures unravel the basis for synthesis and co-transcriptional modification of poxvirus RNA. | |||
Structural Basis of Poxvirus Transcription: Transcribing and Capping Vaccinia Complexes.,Hillen HS, Bartuli J, Grimm C, Dienemann C, Bedenk K, Szalay AA, Fischer U, Cramer P Cell. 2019 Dec 12;179(7):1525-1536.e12. doi: 10.1016/j.cell.2019.11.023. PMID:31835031<ref>PMID:31835031</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6rid" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: DNA-directed RNA polymerase]] | [[Category: DNA-directed RNA polymerase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Vaccinia virus glv-1h68]] | |||
[[Category: Bartuli, J]] | [[Category: Bartuli, J]] | ||
[[Category: Bedenk, K]] | [[Category: Bedenk, K]] | ||
Revision as of 16:13, 25 December 2019
Structure of Vaccinia Virus DNA-dependent RNA polymerase elongation complexStructure of Vaccinia Virus DNA-dependent RNA polymerase elongation complex
Structural highlights
Function[B9U1R2_9POXV] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000746] [B9U1I0_9POXV] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000744] [B9U1M4_9POXV] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000743] Publication Abstract from PubMedPoxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate m(7)G-capped mRNAs in the host cytoplasm. In the accompanying paper, we report structures of core and complete vRNAP complexes of the prototypic Vaccinia poxvirus (Grimm et al., 2019; in this issue of Cell). Here, we present the cryo-electron microscopy (cryo-EM) structures of Vaccinia vRNAP in the form of a transcribing elongation complex and in the form of a co-transcriptional capping complex that contains the viral capping enzyme (CE). The trifunctional CE forms two mobile modules that bind the polymerase surface around the RNA exit tunnel. RNA extends from the vRNAP active site through this tunnel and into the active site of the CE triphosphatase. Structural comparisons suggest that growing RNA triggers large-scale rearrangements on the surface of the transcription machinery during the transition from transcription initiation to RNA capping and elongation. Our structures unravel the basis for synthesis and co-transcriptional modification of poxvirus RNA. Structural Basis of Poxvirus Transcription: Transcribing and Capping Vaccinia Complexes.,Hillen HS, Bartuli J, Grimm C, Dienemann C, Bedenk K, Szalay AA, Fischer U, Cramer P Cell. 2019 Dec 12;179(7):1525-1536.e12. doi: 10.1016/j.cell.2019.11.023. PMID:31835031[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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