1fn9: Difference between revisions

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 ==CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3==
-<StructureSection load='1fn9' size='340' side='right' caption='[[1fn9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1fn9' size='340' side='right'caption='[[1fn9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fn9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Reovirus Reovirus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FN9 FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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>
-<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=1fn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fn9 OCA], [http://pdbe.org/1fn9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fn9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fn9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fn9 ProSAT]</span></td></tr>
+<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>
+<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>
 </table>
+== 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]]
@@ Line 17: / Line 20: @@
 </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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:11230122<ref>PMID:11230122</ref>
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1fn9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Reovirus]]
+[[Category: Large Structures]]
-[[Category: Harrison, S C]]
+[[Category: Reovirus sp]]
-[[Category: Jane-Valbuena, J]]
+[[Category: Harrison SC]]
-[[Category: Nibert, M L]]
+[[Category: Jane-Valbuena J]]
-[[Category: Olland, A M]]
+[[Category: Nibert ML]]
-[[Category: Schiff, L A]]
+[[Category: Olland AM]]
-[[Category: Viral protein]]
+[[Category: Schiff LA]]
-[[Category: Zinc binding motif]]