5lrp: Difference between revisions
New page: '''Unreleased structure''' The entry 5lrp is ON HOLD Authors: Yekwa, E.L., Khourieh, J., Canard, B., Ferron, F. Description: Mopeia Virus Exonuclease domain complexed with Magnesium [[... |
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The | ==Mopeia Virus Exonuclease domain complexed with Magnesium== | ||
<StructureSection load='5lrp' size='340' side='right'caption='[[5lrp]], [[Resolution|resolution]] 1.94Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lrp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mopeia_virus_AN20410 Mopeia virus AN20410]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LRP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.941Å</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=5lrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lrp OCA], [https://pdbe.org/5lrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lrp RCSB], [https://www.ebi.ac.uk/pdbsum/5lrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lrp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5S581_MOPEI Q5S581_MOPEI] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses.[PIRNR:PIRNR004029] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Arenaviridae family is one of the two RNA viral families that encode a 3'-5' exonuclease in their genome. An exonuclease domain is found in the Arenaviridae nucleoprotein and targets dsRNA specifically. This domain is directly involved in suppression of innate immunity in the host cell. Like most phosphate-processing enzymes, it requires a divalent metal ion such as Mg2+ (or Mn2+) as a cofactor to catalyse nucleotide-cleavage and nucleotide-transfer reactions. On the other hand, calcium (Ca2+) inhibits this enzymatic activity, in spite of the fact that Mg2+ and Ca2+ present comparable binding affinities and biological availabilities. Here, the molecular and structural effects of the replacement of magnesium by calcium and its inhibition mechanism for phosphodiester cleavage, an essential reaction in the viral process of innate immunity suppression, are studied. Biochemical data and high-resolution structures of the Mopeia virus exonuclease domain complexed with each ion are reported for the first time. The consequences of the ion swap for the stability of the protein, the catalytic site and the functional role of a specific metal ion in enabling the catalytic cleavage of a dsRNA substrate are outlined. | |||
Activity inhibition and crystal polymorphism induced by active-site metal swapping.,Yekwa E, Khourieh J, Canard B, Papageorgiou N, Ferron F Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):641-649. doi:, 10.1107/S205979831700866X. Epub 2017 Jul 28. PMID:28777079<ref>PMID:28777079</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Canard | <div class="pdbe-citations 5lrp" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mopeia virus AN20410]] | |||
[[Category: Canard B]] | |||
[[Category: Ferron F]] | |||
[[Category: Khourieh J]] | |||
[[Category: Yekwa EL]] | |||
Latest revision as of 21:43, 18 October 2023
Mopeia Virus Exonuclease domain complexed with MagnesiumMopeia Virus Exonuclease domain complexed with Magnesium
Structural highlights
FunctionQ5S581_MOPEI Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses.[PIRNR:PIRNR004029] Publication Abstract from PubMedThe Arenaviridae family is one of the two RNA viral families that encode a 3'-5' exonuclease in their genome. An exonuclease domain is found in the Arenaviridae nucleoprotein and targets dsRNA specifically. This domain is directly involved in suppression of innate immunity in the host cell. Like most phosphate-processing enzymes, it requires a divalent metal ion such as Mg2+ (or Mn2+) as a cofactor to catalyse nucleotide-cleavage and nucleotide-transfer reactions. On the other hand, calcium (Ca2+) inhibits this enzymatic activity, in spite of the fact that Mg2+ and Ca2+ present comparable binding affinities and biological availabilities. Here, the molecular and structural effects of the replacement of magnesium by calcium and its inhibition mechanism for phosphodiester cleavage, an essential reaction in the viral process of innate immunity suppression, are studied. Biochemical data and high-resolution structures of the Mopeia virus exonuclease domain complexed with each ion are reported for the first time. The consequences of the ion swap for the stability of the protein, the catalytic site and the functional role of a specific metal ion in enabling the catalytic cleavage of a dsRNA substrate are outlined. Activity inhibition and crystal polymorphism induced by active-site metal swapping.,Yekwa E, Khourieh J, Canard B, Papageorgiou N, Ferron F Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):641-649. doi:, 10.1107/S205979831700866X. Epub 2017 Jul 28. PMID:28777079[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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