1tme
From Proteopedia
(Difference between revisions)
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<StructureSection load='1tme' size='340' side='right'caption='[[1tme]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1tme' size='340' side='right'caption='[[1tme]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1tme]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1tme]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Theiler's_encephalomyelitis_virus_(STRAIN_DA) Theiler's encephalomyelitis virus (STRAIN DA)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TME FirstGlance]. <br> |
| - | </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=1tme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tme OCA], [https://pdbe.org/1tme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tme RCSB], [https://www.ebi.ac.uk/pdbsum/1tme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tme ProSAT]</span></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]] 2.8Å</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=1tme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tme OCA], [https://pdbe.org/1tme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tme RCSB], [https://www.ebi.ac.uk/pdbsum/1tme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tme ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/POLG_TMEVD POLG_TMEVD] Leader protein: promotes host NUP98 phosphorylation and blocks the export of host mRNA from the nucleus. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. The leader protein also inhibit host interferon regulatory factor 3 (IRF3) dimerization, thereby blocking the transcriptional activation of IFN genes.<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> Protein VP0: VP0 precursor is a component of immature procapsids (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> Protein 2B: Affects membrane integrity and cause an increase in membrane permeability (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function (By similarity).<ref>PMID:19088287</ref> <ref>PMID:19710133</ref> | |
== 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=1tme 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=1tme ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Theiler murine encephalomyelitis virus strains are categorized into two groups, a neurovirulent group that rapidly kills the host, and a demyelinating group that causes a generally nonlethal infection of motor neurons followed by a persistent infection of the white matter with demyelinating lesions similar to those found in multiple sclerosis. The three-dimensional structure of the DA strain, a member of the demyelinating group, has been determined at 2.8 A resolution. As in other picornaviruses, the icosahedral capsid is formed by the packing of wedge-shaped eight-stranded antiparallel beta barrels. The surface of Theiler virus has large star-shaped plateaus at the fivefold axes and broad depressions spanning the twofold axes. Several unusual structural features are clustered near one edge of the depression. These include two finger-like loops projecting from the surface (one formed by residues 78-85 of VP1, and the other formed by residues 56-65 of VP3) and a third loop containing three cysteines (residues 87, 89, and 91 of VP3), which appear to be covalently modified. Most of the sequence differences between the demyelinating and neurovirulent groups that could play a role in determining pathogenesis map to the surface of the star-shaped plateau. The distribution of these sequence differences on the surface of the virion is consistent with models in which the differences in the pathogenesis of the two groups of Theiler viruses are the result of differences in immunological or receptor-mediated recognition processes. | ||
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| - | Three-dimensional structure of Theiler virus.,Grant RA, Filman DJ, Fujinami RS, Icenogle JP, Hogle JM Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2061-5. PMID:1549565<ref>PMID:1549565</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1tme" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Filman | + | [[Category: Filman DJ]] |
| - | [[Category: Grant | + | [[Category: Grant RA]] |
| - | [[Category: Hogle | + | [[Category: Hogle JM]] |
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Current revision
THREE-DIMENSIONAL STRUCTURE OF THEILER VIRUS
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