8b8v: Difference between revisions
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==Crystal structure of the Rabies virus RNA free nucleoprotein- phosphoprotein complex== | |||
<StructureSection load='8b8v' size='340' side='right'caption='[[8b8v]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8b8v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rabies_lyssavirus Rabies lyssavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8B8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B8V FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8b8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b8v OCA], [https://pdbe.org/8b8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b8v RCSB], [https://www.ebi.ac.uk/pdbsum/8b8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b8v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D6Q0Q6_9RHAB D6Q0Q6_9RHAB] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
As for all non-segmented negative RNA viruses, rabies virus has its genome packaged in a linear assembly of nucleoprotein (N), named nucleocapsid. The formation of new nucleocapsids during virus replication in cells requires the production of soluble N protein in complex with its phosphoprotein (P) chaperone. In this study, we reconstituted a soluble heterodimeric complex between an armless N protein of rabies virus (RABV), lacking its N-terminal subdomain (N(NT-ARM)), and a peptide encompassing the N(0) chaperon module of the P protein. We showed that the chaperone module undergoes a disordered-order transition when it assembles with N(0) and measured an affinity in the low nanomolar range using a competition assay. We solved the crystal structure of the complex at a resolution of 2.3 A, unveiling the details of the conserved interfaces. MD simulations showed that both the chaperon module of P and RNA-mediated polymerization reduced the ability of the RNA binding cavity to open and close. Finally, by reconstituting a complex with full-length P protein, we demonstrated that each P dimer could independently chaperon two N(0) molecules. | |||
Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module.,Gerard FCA, Bourhis JM, Mas C, Branchard A, Vu DD, Varhoshkova S, Leyrat C, Jamin M Viruses. 2022 Dec 16;14(12):2813. doi: 10.3390/v14122813. PMID:36560817<ref>PMID:36560817</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bourhis | <div class="pdbe-citations 8b8v" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rabies lyssavirus]] | |||
[[Category: Bourhis JM]] | |||
[[Category: Gerard FCA]] | |||
[[Category: Jamin M]] | |||
Revision as of 12:51, 15 March 2023
Crystal structure of the Rabies virus RNA free nucleoprotein- phosphoprotein complexCrystal structure of the Rabies virus RNA free nucleoprotein- phosphoprotein complex
Structural highlights
FunctionPublication Abstract from PubMedAs for all non-segmented negative RNA viruses, rabies virus has its genome packaged in a linear assembly of nucleoprotein (N), named nucleocapsid. The formation of new nucleocapsids during virus replication in cells requires the production of soluble N protein in complex with its phosphoprotein (P) chaperone. In this study, we reconstituted a soluble heterodimeric complex between an armless N protein of rabies virus (RABV), lacking its N-terminal subdomain (N(NT-ARM)), and a peptide encompassing the N(0) chaperon module of the P protein. We showed that the chaperone module undergoes a disordered-order transition when it assembles with N(0) and measured an affinity in the low nanomolar range using a competition assay. We solved the crystal structure of the complex at a resolution of 2.3 A, unveiling the details of the conserved interfaces. MD simulations showed that both the chaperon module of P and RNA-mediated polymerization reduced the ability of the RNA binding cavity to open and close. Finally, by reconstituting a complex with full-length P protein, we demonstrated that each P dimer could independently chaperon two N(0) molecules. Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module.,Gerard FCA, Bourhis JM, Mas C, Branchard A, Vu DD, Varhoshkova S, Leyrat C, Jamin M Viruses. 2022 Dec 16;14(12):2813. doi: 10.3390/v14122813. PMID:36560817[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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