8pdr

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<StructureSection load='8pdr' size='340' side='right'caption='[[8pdr]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<StructureSection load='8pdr' size='340' side='right'caption='[[8pdr]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[8pdr]] is a 33 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=8PDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PDR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[8pdr]] is a 33 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=8PDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PDR 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&#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&#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=8pdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pdr OCA], [https://pdbe.org/8pdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pdr RCSB], [https://www.ebi.ac.uk/pdbsum/8pdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pdr 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=8pdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pdr OCA], [https://pdbe.org/8pdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pdr RCSB], [https://www.ebi.ac.uk/pdbsum/8pdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pdr ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[https://www.uniprot.org/uniprot/Q91F57_9MONO Q91F57_9MONO]
 
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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 8pdr" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__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

Rigid body fit of assembled HMPV N-RNA spiral bound to the C-terminal region of P

PDB ID 8pdr

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