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| <StructureSection load='7oe3' size='340' side='right'caption='[[7oe3]], [[Resolution|resolution]] 3.35Å' scene=''> | | <StructureSection load='7oe3' size='340' side='right'caption='[[7oe3]], [[Resolution|resolution]] 3.35Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7oe3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OE3 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OE3 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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 3.35Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7och|7och]]</div></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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7oe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oe3 OCA], [https://pdbe.org/7oe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oe3 RCSB], [https://www.ebi.ac.uk/pdbsum/7oe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oe3 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=7oe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oe3 OCA], [https://pdbe.org/7oe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oe3 RCSB], [https://www.ebi.ac.uk/pdbsum/7oe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oe3 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
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| [[https://www.uniprot.org/uniprot/A0A3S8NV63_9VIRU A0A3S8NV63_9VIRU]] RNA-dependent RNA polymerase which is responsible for replication and transcription of the viral RNA genome. During transcription, synthesizes 4 subgenomic RNAs, and assures their capping by a cap-snatching mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.[HAMAP-Rule:MF_04086][PIRNR:PIRNR000836]
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Lassa virus is endemic in West Africa and can cause severe hemorrhagic fever. The viral L protein transcribes and replicates the RNA genome via its RNA-dependent RNA polymerase activity. Here, we present nine cryo-EM structures of the L protein in the apo-, promoter-bound pre-initiation and active RNA synthesis states. We characterize distinct binding pockets for the conserved 3' and 5' promoter RNAs and show how full-promoter binding induces a distinct pre-initiation conformation. In the apo- and early elongation states, the endonuclease is inhibited by two distinct L protein peptides, whereas in the pre-initiation state it is uninhibited. In the early elongation state, a template-product duplex is bound in the active site cavity together with an incoming non-hydrolysable nucleotide and the full C-terminal region of the L protein, including the putative cap-binding domain, is well-ordered. These data advance our mechanistic understanding of how this flexible and multifunctional molecular machine is activated.
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| Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity.,Kouba T, Vogel D, Thorkelsson SR, Quemin ERJ, Williams HM, Milewski M, Busch C, Gunther S, Grunewald K, Rosenthal M, Cusack S Nat Commun. 2021 Dec 2;12(1):7018. doi: 10.1038/s41467-021-27305-5. PMID:34857749<ref>PMID:34857749</ref>
| | ==See Also== |
| | | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7oe3" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Busch, C]] | | [[Category: Busch C]] |
| [[Category: Cusack, S]] | | [[Category: Cusack S]] |
| [[Category: Grunewald, K]] | | [[Category: Grunewald K]] |
| [[Category: Gunther, S]] | | [[Category: Gunther S]] |
| [[Category: Kouba, T]] | | [[Category: Kouba T]] |
| [[Category: Milewski, M]] | | [[Category: Milewski M]] |
| [[Category: Quemin, E]] | | [[Category: Quemin E]] |
| [[Category: Rosenthal, M]] | | [[Category: Rosenthal M]] |
| [[Category: Thorkelsson, S]] | | [[Category: Thorkelsson S]] |
| [[Category: Vogel, D]] | | [[Category: Vogel D]] |
| [[Category: William, H]] | | [[Category: William H]] |
| [[Category: Lassa virus rna-dependent rna polymerase viral rna]]
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| [[Category: Viral protein]]
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