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| | <StructureSection load='6tu5' size='340' side='right'caption='[[6tu5]], [[Resolution|resolution]] 3.33Å' scene=''> | | <StructureSection load='6tu5' size='340' side='right'caption='[[6tu5]], [[Resolution|resolution]] 3.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tu5]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/zhejiang/dtid-zju01/2013(h7n9)) Influenza a virus (a/zhejiang/dtid-zju01/2013(h7n9))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TU5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TU5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tu5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Zhejiang/DTID-ZJU01/2013(H7N9)) Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TU5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.325Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1318616 Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))]), PB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1318616 Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))]), PB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1318616 Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=6tu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tu5 OCA], [https://pdbe.org/6tu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tu5 RCSB], [https://www.ebi.ac.uk/pdbsum/6tu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tu5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tu5 OCA], [http://pdbe.org/6tu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tu5 RCSB], [http://www.ebi.ac.uk/pdbsum/6tu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tu5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/M9TI86_9INFA M9TI86_9INFA]] Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.[HAMAP-Rule:MF_04063][SAAS:SAAS00956500] [[http://www.uniprot.org/uniprot/X5F427_9INFA X5F427_9INFA]] Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex.[HAMAP-Rule:MF_04062][SAAS:SAAS01109044] [[http://www.uniprot.org/uniprot/M9TLW3_9INFA M9TLW3_9INFA]] RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copies vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs.[HAMAP-Rule:MF_04065] | + | [https://www.uniprot.org/uniprot/M9TI86_9INFA M9TI86_9INFA] Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.[HAMAP-Rule:MF_04063][SAAS:SAAS00956500] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RNA-directed RNA polymerase]]
| + | [[Category: Cusack S]] |
| - | [[Category: Cusack, S]] | + | [[Category: Pflug A]] |
| - | [[Category: Pflug, A]] | + | |
| - | [[Category: Rna-dependent rna polymerase]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
M9TI86_9INFA Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.[HAMAP-Rule:MF_04063][SAAS:SAAS00956500]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wandzik JM, Kouba T, Karuppasamy M, Pflug A, Drncova P, Provaznik J, Azevedo N, Cusack S. A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase. Cell. 2020 Apr 16. pii: S0092-8674(20)30389-5. doi: 10.1016/j.cell.2020.03.061. PMID:32304664 doi:http://dx.doi.org/10.1016/j.cell.2020.03.061
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