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[[Image:1fn9.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3==
|PDB= 1fn9 |SIZE=350|CAPTION= <scene name='initialview01'>1fn9</scene>, resolution 1.8&Aring;
<StructureSection load='1fn9' size='340' side='right'caption='[[1fn9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[1fn9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FN9 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fn9 OCA], [https://pdbe.org/1fn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fn9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fn9 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fn9 OCA], [http://www.ebi.ac.uk/pdbsum/1fn9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fn9 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/SIGM3_REOVD SIGM3_REOVD] Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2/PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding.<ref>PMID:9268168</ref>  The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fn/1fn9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fn9 ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3'''
==See Also==
 
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 
== References ==
==Overview==
<references/>
The crystallographically determined structure of the reovirus outer capsid protein sigma3 reveals a two-lobed structure organized around a long central helix. The smaller of the two lobes includes a CCHC zinc-binding site. Residues that vary between strains and serotypes lie mainly on one surface of the protein; residues on the opposite surface are conserved. From a fit of this model to a reconstruction of the whole virion from electron cryomicroscopy, we propose that each sigma3 subunit is positioned with the small lobe anchoring it to the protein mu1 on the surface of the virion, and the large lobe, the site of initial cleavages during entry-related proteolytic disassembly, protruding outwards. The surface containing variable residues faces solvent. The crystallographic asymmetric unit contains two sigma3 subunits, tightly associated as a dimer. One broad surface of the dimer has a positively charged surface patch, which extends across the dyad. In infected cells, sigma3 binds dsRNA and inhibits the interferon response. The location and extent of the positively charged surface patch suggest that the dimer is the RNA-binding form of sigma3.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1FN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FN9 OCA].
[[Category: Reovirus sp]]
 
[[Category: Harrison SC]]
==Reference==
[[Category: Jane-Valbuena J]]
Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution., Olland AM, Jane-Valbuena J, Schiff LA, Nibert ML, Harrison SC, EMBO J. 2001 Mar 1;20(5):979-89. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11230122 11230122]
[[Category: Nibert ML]]
[[Category: Reovirus sp.]]
[[Category: Olland AM]]
[[Category: Single protein]]
[[Category: Schiff LA]]
[[Category: Harrison, S C.]]
[[Category: Jane-Valbuena, J.]]
[[Category: Nibert, M L.]]
[[Category: Olland, A M.]]
[[Category: Schiff, L A.]]
[[Category: zinc binding motif]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:17 2008''

Latest revision as of 10:16, 7 February 2024

CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3

Structural highlights

1fn9 is a 2 chain structure with sequence from Reovirus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SIGM3_REOVD Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2/PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding.[1] The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.

Evolutionary Conservation

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

See Also

References

  1. ↑ Yue Z, Shatkin AJ. Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins. Virology. 1997 Aug 4;234(2):364-71. PMID:9268168 doi:10.1006/viro.1997.8664

1fn9, resolution 1.80Å

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