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| | ==Crystal structure of the N-terminal domain of the PA subunit of Thogoto virus polymerase (form 1)== | | ==Crystal structure of the N-terminal domain of the PA subunit of Thogoto virus polymerase (form 1)== |
| - | <StructureSection load='4cgx' size='340' side='right' caption='[[4cgx]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4cgx' size='340' side='right'caption='[[4cgx]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cgx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thogoto_virus Thogoto virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cgx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thogoto_thogotovirus Thogoto thogotovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CGX FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cgs|4cgs]], [[4chc|4chc]], [[4chd|4chd]], [[4che|4che]], [[4chf|4chf]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4cgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgx RCSB], [http://www.ebi.ac.uk/pdbsum/4cgx PDBsum]</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=4cgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgx OCA], [https://pdbe.org/4cgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cgx RCSB], [https://www.ebi.ac.uk/pdbsum/4cgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PA_THOGV PA_THOGV]] Initiates transcription by a unique cap-stealing mechanism that involves the cleavage of only the m(7)GpppAm structure from cellular hnRNAs. | + | [https://www.uniprot.org/uniprot/PA_THOGV PA_THOGV] Initiates transcription by a unique cap-stealing mechanism that involves the cleavage of only the m(7)GpppAm structure from cellular hnRNAs. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4cgx" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thogoto virus]] | + | [[Category: Large Structures]] |
| - | [[Category: Bouvier, D]] | + | [[Category: Thogoto thogotovirus]] |
| - | [[Category: Crepin, T]] | + | [[Category: Bouvier D]] |
| - | [[Category: Cusack, S]] | + | [[Category: Crepin T]] |
| - | [[Category: Guilligay, D]] | + | [[Category: Cusack S]] |
| - | [[Category: Kadlec, J]] | + | [[Category: Guilligay D]] |
| - | [[Category: Kochs, G]] | + | [[Category: Kadlec J]] |
| - | [[Category: Lunardi, T]] | + | [[Category: Kochs G]] |
| - | [[Category: Ruigrok, R W.H]] | + | [[Category: Lunardi T]] |
| - | [[Category: Transcription]]
| + | [[Category: Ruigrok RWH]] |
| Structural highlights
Function
PA_THOGV Initiates transcription by a unique cap-stealing mechanism that involves the cleavage of only the m(7)GpppAm structure from cellular hnRNAs.
Publication Abstract from PubMed
Orthomyxovirus Influenza A virus (IAV) heterotrimeric polymerase performs transcription of viral mRNAs by cap-snatching, which involves generation of capped primers by host pre-mRNA binding via the PB2 subunit cap-binding site and cleavage 10-13 nucleotides from the 5' cap by the PA subunit endonuclease. Thogotoviruses, tick-borne orthomyxoviruses that includes Thogoto (THOV), Dhori (DHOV) and Jos (JOSV) viruses, are thought to perform cap-snatching by cleaving directly after the cap and thus have no heterogeneous, host-derived sequences at the 5' extremity of their mRNAs. Based on recent work identifying the cap-binding and endonuclease domains in IAV polymerase, we determined the crystal structures of two THOV PB2 domains, the putative cap-binding and the so-called '627-domain', and the structures of the putative endonuclease domains (PA-Nter) of THOV and DHOV. Despite low sequence similarity, corresponding domains have the same fold confirming the overall architectural similarity of orthomyxovirus polymerases. However the putative Thogotovirus cap-snatching domains in PA and PB2 have non-conservative substitutions of key active site residues. Biochemical analysis confirms that, unlike the IAV domains, the THOV and DHOV PA-Nter domains do not bind divalent cations and have no endonuclease activity and the THOV central PB2 domain does not bind cap analogues. On the other hand, sequence analysis suggests that other, non-influenza, orthomyxoviruses, such as salmon anemia virus (isavirus) and Quaranfil virus likely conserve active cap-snatching domains correlating with the reported occurrence of heterogeneous, host-derived sequences at the 5' end of the mRNAs of these viruses. These results highlight the unusual nature of transcription initiation by Thogotoviruses.
Comparative structural and functional analysis of orthomyxovirus polymerase cap-snatching domains.,Guilligay D, Kadlec J, Crepin T, Lunardi T, Bouvier D, Kochs G, Ruigrok RW, Cusack S PLoS One. 2014 Jan 15;9(1):e84973. doi: 10.1371/journal.pone.0084973. eCollection, 2014 Jan 15. PMID:24454773[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Guilligay D, Kadlec J, Crepin T, Lunardi T, Bouvier D, Kochs G, Ruigrok RW, Cusack S. Comparative structural and functional analysis of orthomyxovirus polymerase cap-snatching domains. PLoS One. 2014 Jan 15;9(1):e84973. doi: 10.1371/journal.pone.0084973. eCollection, 2014 Jan 15. PMID:24454773 doi:http://dx.doi.org/10.1371/journal.pone.0084973
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