6tw1
From Proteopedia
(Difference between revisions)
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<StructureSection load='6tw1' size='340' side='right'caption='[[6tw1]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='6tw1' size='340' side='right'caption='[[6tw1]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TW1 FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M4H:5-oxidanyl-4-oxidanylidene-1-[(1-pyrrolo[2,3-b]pyridin-1-ylcyclopentyl)methyl]pyridine-3-carboxylic+acid'>M4H</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M4H:5-oxidanyl-4-oxidanylidene-1-[(1-pyrrolo[2,3-b]pyridin-1-ylcyclopentyl)methyl]pyridine-3-carboxylic+acid'>M4H</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></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=6tw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tw1 OCA], [https://pdbe.org/6tw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tw1 RCSB], [https://www.ebi.ac.uk/pdbsum/6tw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tw1 ProSAT]</span></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=6tw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tw1 OCA], [https://pdbe.org/6tw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tw1 RCSB], [https://www.ebi.ac.uk/pdbsum/6tw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tw1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Function == | ||
- | [https://www.uniprot.org/uniprot/H6QM91_9INFA H6QM91_9INFA] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Influenza polymerase uses unique mechanisms to synthesize capped and polyadenylated mRNAs from the genomic viral RNA (vRNA) template, which is packaged inside ribonucleoprotein particles (vRNPs). Here, we visualize by cryoelectron microscopy the conformational dynamics of the polymerase during the complete transcription cycle from pre-initiation to termination, focusing on the template trajectory. After exiting the active site cavity, the template 3' extremity rebinds into a specific site on the polymerase surface. Here, it remains sequestered during all subsequent transcription steps, forcing the template to loop out as it further translocates. At termination, the strained connection between the bound template 5' end and the active site results in polyadenylation by stuttering at uridine 17. Upon product dissociation, further conformational changes release the trapped template, allowing recycling back into the pre-initiation state. Influenza polymerase thus performs transcription while tightly binding to and protecting both template ends, allowing efficient production of multiple mRNAs from a single vRNP. | ||
- | |||
- | A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase.,Wandzik JM, Kouba T, Karuppasamy M, Pflug A, Drncova P, Provaznik J, Azevedo N, Cusack S Cell. 2020 Apr 16. pii: S0092-8674(20)30389-5. doi: 10.1016/j.cell.2020.03.061. PMID:32304664<ref>PMID:32304664</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 6tw1" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Influenza B virus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cusack S]] | [[Category: Cusack S]] | ||
[[Category: Kouba T]] | [[Category: Kouba T]] | ||
[[Category: Wandzik JM]] | [[Category: Wandzik JM]] |
Current revision
Bat Influenza A polymerase termination complex with pyrophosphate using 44-mer vRNA template with mutated oligo(U) sequence
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