8pdn

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<StructureSection load='8pdn' size='340' side='right'caption='[[8pdn]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
<StructureSection load='8pdn' size='340' side='right'caption='[[8pdn]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[8pdn]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Human_metapneumovirus_A Human metapneumovirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PDN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[8pdn]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Human_metapneumovirus_CAN97-83 Human metapneumovirus CAN97-83]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PDN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.7&#8491;</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]] 4.7&#8491;</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=8pdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pdn OCA], [https://pdbe.org/8pdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pdn RCSB], [https://www.ebi.ac.uk/pdbsum/8pdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pdn 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=8pdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pdn OCA], [https://pdbe.org/8pdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pdn RCSB], [https://www.ebi.ac.uk/pdbsum/8pdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pdn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/Q91F57_9MONO Q91F57_9MONO]
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[https://www.uniprot.org/uniprot/NCAP_HMPVC NCAP_HMPVC] Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication.[UniProtKB:P03418]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human metapneumovirus (HMPV) is a major cause of respiratory illness in young children. The HMPV polymerase (L) binds an obligate cofactor, the phosphoprotein (P). During replication and transcription, the L/P complex traverses the viral RNA genome, which is encapsidated within nucleoproteins (N). An essential interaction between N and a C-terminal region of P tethers the L/P polymerase to the template. This N-P interaction is also involved in the formation of cytoplasmic viral factories in infected cells, called inclusion bodies. To define how the polymerase component P recognizes N-encapsidated RNA (N-RNA) we employed cryogenic electron microscopy (cryo-EM) and molecular dynamics simulations, coupled to activity assays and imaging of inclusion bodies in cells. We report a 2.9 A resolution structure of a triple-complex between multimeric N, bound to both RNA and the C-terminal region of P. Furthermore, we also present cryo-EM structures of assembled N in different oligomeric states, highlighting the plasticity of N. Combined with our functional assays, these structural data delineate in molecular detail how P attaches to N-RNA whilst retaining substantial conformational dynamics. Moreover, the N-RNA-P triple complex structure provides a molecular blueprint for the design of therapeutics to potentially disrupt the attachment of L/P to its template.
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Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus.,Whitehead JD, Decool H, Leyrat C, Carrique L, Fix J, Eleouet JF, Galloux M, Renner M Nat Commun. 2023 Nov 22;14(1):7627. doi: 10.1038/s41467-023-43434-5. PMID:37993464<ref>PMID:37993464</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8pdn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Human metapneumovirus A]]
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[[Category: Human metapneumovirus CAN97-83]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Carrique L]]
[[Category: Carrique L]]

Current revision

Spiral of assembled human metapneumovirus (HMPV) N-RNA

PDB ID 8pdn

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