4idu: Difference between revisions
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<StructureSection load='4idu' size='340' side='right'caption='[[4idu]], [[Resolution|resolution]] 3.08Å' scene=''> | <StructureSection load='4idu' size='340' side='right'caption='[[4idu]], [[Resolution|resolution]] 3.08Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4idu]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4idu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schmallenberg_virus Schmallenberg virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IDU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4idu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idu OCA], [https://pdbe.org/4idu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4idu RCSB], [https://www.ebi.ac.uk/pdbsum/4idu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4idu ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/NCAP_SBVBH NCAP_SBVBH] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Nucleoprotein|Nucleoprotein]] | *[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Schmallenberg virus]] | [[Category: Schmallenberg virus]] | ||
[[Category: Dong C]] | |||
[[Category: Dong H]] | |||
[[Category: Elliott RM]] | |||
[[Category: Li P]] | |||
Revision as of 12:03, 9 November 2022
crystal structure of Schmallenberg virus nucleoproteincrystal structure of Schmallenberg virus nucleoprotein
Structural highlights
FunctionNCAP_SBVBH Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) (By similarity). Publication Abstract from PubMedSchmallenberg virus (SBV), a newly emerged orthobunyavirus (family Bunyaviridae), has spread rapidly across Europe, and has caused congenital abnormalities in the offspring of cattle, sheep and goats. Like other orthobunyaviruses, SBV contains a tripartite negative-sense RNA genome that encodes four structural and two nonstructural proteins. The nucleoprotein (N) encapsidates the three viral genomic RNA segments and plays a crucial role in viral RNA transcription and replication. Here we report the crystal structure of bacterially-expressed SBV nucleoprotein to 3.06A resolution. The protomer is composed of two domains (N-terminal and C-terminal domains) with flexible N-terminal and C-terminal arms. The N protein has a novel fold, and forms a central positively charged cleft for genomic RNA binding. The nucleoprotein purified under native conditions forms a tetramer, while the nucleoprotein obtained following denaturation and refolding forms a hexamer. Our structural and functional analyses demonstrate that both N-terminal and C-terminal arms are involved in N-N interaction and oligomerization and play an essential role in viral RNA synthesis, suggesting a novel mechanism for viral RNA encapsidation and transcription. Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism for genome encapsidation.,Dong H, Li P, Elliott RM, Dong C J Virol. 2013 Mar 6. PMID:23468499[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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