7oe3: Difference between revisions
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==Apo-structure of Lassa virus L protein (well-resolved endonuclease) [APO-ENDO]== | ==Apo-structure of Lassa virus L protein (well-resolved endonuclease) [APO-ENDO]== | ||
<StructureSection load='7oe3' size='340' side='right'caption='[[7oe3]]' scene=''> | <StructureSection load='7oe3' size='340' side='right'caption='[[7oe3]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
</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> | </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='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='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 == | |||
[[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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7oe3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__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]] | |||
[[Category: Viral protein]] | |||