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==Structure of RNA-bound decameric HMPV nucleoprotein==
==Structure of RNA-bound decameric HMPV nucleoprotein==
<StructureSection load='5fvc' size='340' side='right' caption='[[5fvc]], [[Resolution|resolution]] 4.17&Aring;' scene=''>
<StructureSection load='5fvc' size='340' side='right'caption='[[5fvc]], [[Resolution|resolution]] 4.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5fvc]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FVC FirstGlance]. <br>
<table><tr><td colspan='2'>[[5fvc]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [https://en.wikipedia.org/wiki/Human_metapneumovirus Human metapneumovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FVC FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fvd|5fvd]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.17&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvc OCA], [http://pdbe.org/5fvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvc RCSB], [http://www.ebi.ac.uk/pdbsum/5fvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvc 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=5fvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvc OCA], [https://pdbe.org/5fvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fvc RCSB], [https://www.ebi.ac.uk/pdbsum/5fvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvc ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q91F57_9MONO Q91F57_9MONO]
Non-segmented, (-)RNA viruses cause serious human diseases. Human metapneumovirus (HMPV), an emerging pathogen of this order of viruses (Mononegavirales) is one of the main causes of respiratory tract illness in children. To help elucidate the assembly mechanism of the nucleocapsid (the viral RNA genome packaged by the nucleoprotein N) we present crystallographic structures of HMPV N in its assembled RNA-bound state and in a monomeric state, bound to the polymerase cofactor P. Our structures reveal molecular details of how P inhibits the self-assembly of N and how N transitions between the RNA-free and RNA-bound conformational state. Notably, we observe a role for the C-terminal extension of N in directly preventing premature uptake of RNA by inserting into the RNA-binding cleft.Our structures suggest a common mechanism of how the growth of the nucleocapsid is orchestrated, and highlight an interaction site representing an important target for antivirals.


Nucleocapsid assembly in pneumoviruses is regulated by conformational switching of the N protein.,Renner M, Bertinelli M, Leyrat C, Paesen GC, Saraiva de Oliveira LF, Huiskonen JT, Grimes JM Elife. 2016 Feb 16;5. pii: e12627. doi: 10.7554/eLife.12627. PMID:26880565<ref>PMID:26880565</ref>
==See Also==
 
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fvc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Human metapneumovirus]]
[[Category: Bertinelli, M]]
[[Category: Large Structures]]
[[Category: Grimes, J M]]
[[Category: Bertinelli M]]
[[Category: Huiskonen, J T]]
[[Category: Grimes JM]]
[[Category: Leyrat, C]]
[[Category: Huiskonen JT]]
[[Category: Oliveira, L F.Saraiva de]]
[[Category: Leyrat C]]
[[Category: Paesen, G C]]
[[Category: Paesen GC]]
[[Category: Renner, M]]
[[Category: Renner M]]
[[Category: Mononegavirale]]
[[Category: Saraiva de Oliveira LF]]
[[Category: Nucleoprotein]]
[[Category: Pneumovirus]]
[[Category: Viral protein]]

Latest revision as of 10:23, 1 May 2024

Structure of RNA-bound decameric HMPV nucleoproteinStructure of RNA-bound decameric HMPV nucleoprotein

Structural highlights

5fvc is a 11 chain structure with sequence from Escherichia coli BL21(DE3) and Human metapneumovirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.17Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q91F57_9MONO

See Also

5fvc, resolution 4.17Å

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