6yi3: Difference between revisions
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<StructureSection load='6yi3' size='340' side='right'caption='[[6yi3]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | <StructureSection load='6yi3' size='340' side='right'caption='[[6yi3]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6yi3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[6yi3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YI3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YI3 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yi3 OCA], [http://pdbe.org/6yi3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yi3 RCSB], [http://www.ebi.ac.uk/pdbsum/6yi3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yi3 ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yi3 OCA], [http://pdbe.org/6yi3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yi3 RCSB], [http://www.ebi.ac.uk/pdbsum/6yi3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yi3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/NCAP_SARS2 NCAP_SARS2]] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. | [[http://www.uniprot.org/uniprot/NCAP_SARS2 NCAP_SARS2]] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the coronavirus disease 2019 (COVID-19). SARS-CoV-2 is a single-stranded positive-sense RNA virus. Like other coronaviruses, SARS-CoV-2 has an unusually large genome that encodes four structural proteins and sixteen nonstructural proteins. The structural nucleocapsid phosphoprotein N is essential for linking the viral genome to the viral membrane. Both N-terminal RNA binding (N-NTD) and C-terminal dimerization domains are involved in capturing the RNA genome and, the intrinsically disordered region between these domains anchors the ribonucleoprotein complex to the viral membrane. Here, we characterized the structure of the N-NTD and its interaction with RNA using NMR spectroscopy. We observed a positively charged canyon on the surface of the N-NTD that might serve as a putative RNA binding site similarly to other coronaviruses. The subsequent NMR titrations using single-stranded and double-stranded RNA revealed a much more extensive U-shaped RNA-binding cleft lined with regularly distributed arginines and lysines. The NMR data supported by mutational analysis allowed us to construct hybrid atomic models of the N-NTD/RNA complex that provided detailed insight into RNA recognition. | |||
Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein.,Dinesh DC, Chalupska D, Silhan J, Koutna E, Nencka R, Veverka V, Boura E PLoS Pathog. 2020 Dec 2;16(12):e1009100. doi: 10.1371/journal.ppat.1009100., eCollection 2020 Dec. PMID:33264373<ref>PMID:33264373</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6yi3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: 2019-ncov]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boura, E]] | [[Category: Boura, E]] | ||
[[Category: Veverka, V]] | [[Category: Veverka, V]] | ||
Revision as of 09:58, 30 December 2020
The N-terminal RNA-binding domain of the SARS-CoV-2 nucleocapsid phosphoproteinThe N-terminal RNA-binding domain of the SARS-CoV-2 nucleocapsid phosphoprotein
Structural highlights
Function[NCAP_SARS2] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Publication Abstract from PubMedSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the coronavirus disease 2019 (COVID-19). SARS-CoV-2 is a single-stranded positive-sense RNA virus. Like other coronaviruses, SARS-CoV-2 has an unusually large genome that encodes four structural proteins and sixteen nonstructural proteins. The structural nucleocapsid phosphoprotein N is essential for linking the viral genome to the viral membrane. Both N-terminal RNA binding (N-NTD) and C-terminal dimerization domains are involved in capturing the RNA genome and, the intrinsically disordered region between these domains anchors the ribonucleoprotein complex to the viral membrane. Here, we characterized the structure of the N-NTD and its interaction with RNA using NMR spectroscopy. We observed a positively charged canyon on the surface of the N-NTD that might serve as a putative RNA binding site similarly to other coronaviruses. The subsequent NMR titrations using single-stranded and double-stranded RNA revealed a much more extensive U-shaped RNA-binding cleft lined with regularly distributed arginines and lysines. The NMR data supported by mutational analysis allowed us to construct hybrid atomic models of the N-NTD/RNA complex that provided detailed insight into RNA recognition. Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein.,Dinesh DC, Chalupska D, Silhan J, Koutna E, Nencka R, Veverka V, Boura E PLoS Pathog. 2020 Dec 2;16(12):e1009100. doi: 10.1371/journal.ppat.1009100., eCollection 2020 Dec. PMID:33264373[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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