1f8v

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<StructureSection load='1f8v' size='340' side='right'caption='[[1f8v]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1f8v' size='340' side='right'caption='[[1f8v]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1f8v]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Pariacato_virus Pariacato virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F8V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1f8v]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Pariacoto_virus Pariacoto virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F8V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bbv|2bbv]], [[1nov|1nov]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=1f8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f8v OCA], [http://pdbe.org/1f8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f8v RCSB], [http://www.ebi.ac.uk/pdbsum/1f8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f8v ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f8v OCA], [https://pdbe.org/1f8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f8v RCSB], [https://www.ebi.ac.uk/pdbsum/1f8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f8v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAPSD_PAV CAPSD_PAV]] Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid protein alpha generating capsid protein beta and the membrane-active peptide gamma (By similarity). Peptide gamma: membrane-permeabilizing peptide produced by virus maturation, thereby creating the infectious virion. After endocytosis into the host cell, peptide gamma is probably exposed in endosomes, where it permeabilizes the endosomal membrane, facilitating translocation of viral capsid or RNA into the cytoplasm (By similarity).
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[https://www.uniprot.org/uniprot/CAPSD_PAV CAPSD_PAV] Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid protein alpha generating capsid protein beta and the membrane-active peptide gamma (By similarity). Peptide gamma: membrane-permeabilizing peptide produced by virus maturation, thereby creating the infectious virion. After endocytosis into the host cell, peptide gamma is probably exposed in endosomes, where it permeabilizes the endosomal membrane, facilitating translocation of viral capsid or RNA into the cytoplasm (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1f8v ConSurf].
</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=1f8v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The 3.0 A resolution crystal structure of Pariacoto virus (PaV) reveals extensive interactions between portions of the viral RNA genome and the icosahedral capsid. Under the protein shell of the T = 3 quasi equivalent capsid lies a dodecahedral cage composed of RNA duplex that accounts for approximately 35% of the single-stranded RNA genome. The highly basic N-terminal regions (residues 7-54) of the subunits, forming pentamers (A subunits) are clearly visible in the density map and make numerous interactions with the RNA cage. The C-terminal segments (residues 394-401) of the A subunits lie in channels near the quasi three-fold axes. Electron cryo-microscopy and image reconstruction of PaV particles clearly show the dodecahedral RNA cage.
 
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The structure of pariacoto virus reveals a dodecahedral cage of duplex RNA.,Tang L, Johnson KN, Ball LA, Lin T, Yeager M, Johnson JE Nat Struct Biol. 2001 Jan;8(1):77-83. PMID:11135676<ref>PMID:11135676</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1f8v" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Virus coat protein|Virus coat protein]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pariacato virus]]
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[[Category: Pariacoto virus]]
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[[Category: Ball, L A]]
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[[Category: Ball LA]]
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[[Category: Johnson, J E]]
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[[Category: Johnson JE]]
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[[Category: Johnson, K N]]
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[[Category: Johnson KN]]
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[[Category: Lin, T]]
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[[Category: Lin T]]
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[[Category: Tang, L]]
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[[Category: Tang L]]
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[[Category: Yeager, M]]
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[[Category: Yeager M]]
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[[Category: Beta-sandwich]]
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[[Category: Coat protein]]
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[[Category: Gamma polypeptide]]
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[[Category: Icosahedral virus]]
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[[Category: Nodavirus]]
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[[Category: Nucleoprotein]]
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[[Category: Protein-rna interaction]]
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[[Category: Rna cage]]
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[[Category: Rna duplex]]
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[[Category: Virus-rna complex]]
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Current revision

THE STRUCTURE OF PARIACOTO VIRUS REVEALS A DODECAHEDRAL CAGE OF DUPLEX RNA

PDB ID 1f8v

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