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==== | ==CryoEM structure of the Nipah virus nucleocapsid single helical turn assembly== | ||
<StructureSection load='7nt5' size='340' side='right'caption='[[7nt5]]' scene=''> | <StructureSection load='7nt5' size='340' side='right'caption='[[7nt5]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7nt5]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [https://en.wikipedia.org/wiki/Henipavirus_nipahense Henipavirus nipahense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NT5 FirstGlance]. <br> | ||
</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=7nt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nt5 OCA], [https://pdbe.org/7nt5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nt5 RCSB], [https://www.ebi.ac.uk/pdbsum/7nt5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nt5 ProSAT]</span></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]] 3.5Å</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=7nt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nt5 OCA], [https://pdbe.org/7nt5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nt5 RCSB], [https://www.ebi.ac.uk/pdbsum/7nt5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nt5 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/NCAP_NIPAV NCAP_NIPAV] Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 A resolution. The helical assembly is stabilised by previously undefined N- and C-terminal segments, contributing to subunit-subunit interactions. RNA is wrapped around the nucleocapsid protein assembly with a periodicity of six nucleotides per protomer, in the "3-bases-in, 3-bases-out" conformation, with protein plasticity enabling non-sequence specific interactions. The structure reveals commonalities in RNA binding pockets and in the conformation of bound RNA, not only with members of the Paramyxoviridae family, but also with the evolutionarily distant Filoviridae Ebola virus. Significant structural differences with other Paramyxoviridae members are also observed, particularly in the position and length of the exposed alpha-helix, residues 123-139, which may serve as a valuable epitope for surveillance and diagnostics. | |||
CryoEM structure of the Nipah virus nucleocapsid assembly.,Ker DS, Jenkins HT, Greive SJ, Antson AA PLoS Pathog. 2021 Jul 16;17(7):e1009740. doi: 10.1371/journal.ppat.1009740. , eCollection 2021 Jul. PMID:34270629<ref>PMID:34270629</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7nt5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Henipavirus nipahense]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Antson AA]] | ||
[[Category: Greive SJ]] | |||
[[Category: Jenkins HT]] | |||
[[Category: Ker DS]] | |||
Latest revision as of 11:58, 14 July 2024
CryoEM structure of the Nipah virus nucleocapsid single helical turn assemblyCryoEM structure of the Nipah virus nucleocapsid single helical turn assembly
Structural highlights
FunctionNCAP_NIPAV Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (By similarity). Publication Abstract from PubMedNipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 A resolution. The helical assembly is stabilised by previously undefined N- and C-terminal segments, contributing to subunit-subunit interactions. RNA is wrapped around the nucleocapsid protein assembly with a periodicity of six nucleotides per protomer, in the "3-bases-in, 3-bases-out" conformation, with protein plasticity enabling non-sequence specific interactions. The structure reveals commonalities in RNA binding pockets and in the conformation of bound RNA, not only with members of the Paramyxoviridae family, but also with the evolutionarily distant Filoviridae Ebola virus. Significant structural differences with other Paramyxoviridae members are also observed, particularly in the position and length of the exposed alpha-helix, residues 123-139, which may serve as a valuable epitope for surveillance and diagnostics. CryoEM structure of the Nipah virus nucleocapsid assembly.,Ker DS, Jenkins HT, Greive SJ, Antson AA PLoS Pathog. 2021 Jul 16;17(7):e1009740. doi: 10.1371/journal.ppat.1009740. , eCollection 2021 Jul. PMID:34270629[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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