2gec: Difference between revisions

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==Structure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangement==
==Structure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangement==
<StructureSection load='2gec' size='340' side='right' caption='[[2gec]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='2gec' size='340' side='right' caption='[[2gec]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2btl|2btl]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2btl|2btl]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11120 Avian infectious bronchitis virus])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11120 Avian infectious bronchitis virus])</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=2gec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gec OCA], [http://pdbe.org/2gec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gec RCSB], [http://www.ebi.ac.uk/pdbsum/2gec PDBsum]</span></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=2gec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gec OCA], [http://pdbe.org/2gec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gec RCSB], [http://www.ebi.ac.uk/pdbsum/2gec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gec ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/2gec_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/2gec_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 10:10, 20 June 2018

Structure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangementStructure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangement

Structural highlights

2gec is a 2 chain structure with sequence from Avian infectious bronchitis virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:N (Avian infectious bronchitis virus)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NCAP_IBVG] Major structural component of virions that associates with genomic RNA to form a long, flexible, helical nucleocapsid. Interaction with the M protein leads to the formation of virus particles. Binds to cellular membranes and phospholipids. Elicits cell-mediated immunity. May play roles in viral transcription and translation, and/or replication.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Coronaviruses cause a variety of respiratory and enteric diseases in animals and humans including severe acute respiratory syndrome. In these enveloped viruses, the filamentous nucleocapsid is formed by the association of nucleocapsid (N) protein with single-stranded viral RNA. The N protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. We describe the structure of the two proteolytically resistant domains of the N protein from infectious bronchitis virus (IBV), a prototype coronavirus. These domains are located at its N- and C-terminal ends (NTD and CTD, respectively). The NTD of the IBV Gray strain at 1.3-A resolution exhibits a U-shaped structure, with two arms rich in basic residues, providing a module for specific interaction with RNA. The CTD forms a tightly intertwined dimer with an intermolecular four-stranded central beta-sheet platform flanked by alpha helices, indicating that the basic building block for coronavirus nucleocapsid formation is a dimeric assembly of N protein. The variety of quaternary arrangements of the NTD and CTD revealed by the analysis of the different crystal forms delineates possible interfaces that could be used for the formation of a flexible filamentous ribonucleocapsid. The striking similarity between the dimeric structure of CTD and the nucleocapsid-forming domain of a distantly related arterivirus indicates a conserved mechanism of nucleocapsid formation for these two viral families.

X-ray structures of the N- and C-terminal domains of a coronavirus nucleocapsid protein: implications for nucleocapsid formation.,Jayaram H, Fan H, Bowman BR, Ooi A, Jayaram J, Collisson EW, Lescar J, Prasad BV J Virol. 2006 Jul;80(13):6612-20. PMID:16775348[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Jayaram H, Fan H, Bowman BR, Ooi A, Jayaram J, Collisson EW, Lescar J, Prasad BV. X-ray structures of the N- and C-terminal domains of a coronavirus nucleocapsid protein: implications for nucleocapsid formation. J Virol. 2006 Jul;80(13):6612-20. PMID:16775348 doi:80/13/6612

2gec, resolution 1.30Å

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OCA