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| | <SX load='6sag' size='340' side='right' viewer='molstar' caption='[[6sag]], [[Resolution|resolution]] 2.00Å' scene=''> | | <SX load='6sag' size='340' side='right' viewer='molstar' caption='[[6sag]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sag]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tmv Tmv] and [http://en.wikipedia.org/wiki/Tobacco_mosaic_virus_(vulgare) Tobacco mosaic virus (vulgare)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SAG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SAG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sag]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tobacco_mosaic_virus_(vulgare) Tobacco mosaic virus (vulgare)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SAG FirstGlance]. <br> |
| - | </td></tr><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=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sag OCA], [http://pdbe.org/6sag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sag RCSB], [http://www.ebi.ac.uk/pdbsum/6sag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sag ProSAT]</span></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=6sag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sag OCA], [https://pdbe.org/6sag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sag RCSB], [https://www.ebi.ac.uk/pdbsum/6sag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sag ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSD_TMV CAPSD_TMV]] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. | + | [https://www.uniprot.org/uniprot/CAPSD_TMV CAPSD_TMV] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | + | *[[Tobacco Mosaic Virus|Tobacco Mosaic Virus]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tmv]]
| + | [[Category: Beckers M]] |
| - | [[Category: Beckers, M]] | + | [[Category: Sachse C]] |
| - | [[Category: Sachse, C]] | + | [[Category: Weis F]] |
| - | [[Category: Weis, F]] | + | |
| - | [[Category: Ca2+ switch]]
| + | |
| - | [[Category: Caspar carboxylate]]
| + | |
| - | [[Category: Virus]]
| + | |
| - | [[Category: Virus assembly/disassembly]]
| + | |
| Structural highlights
Function
CAPSD_TMV Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA.
Publication Abstract from PubMed
Stable capsid structures of viruses protect viral RNA while they also require controlled disassembly for releasing the viral genome in the host cell. A detailed understanding of viral disassembly processes and the involved structural switches is still lacking. This process has been extensively studied using tobacco mosaic virus (TMV), and carboxylate interactions are assumed to play a critical part in this process. Here, we present two cryo-EM structures of the helical TMV assembly at 2.0 and 1.9 A resolution in conditions of high Ca(2+) concentration at low pH and in water. Based on our atomic models, we identify the conformational details of the disassembly switch mechanism: In high Ca(2+) /acidic pH environment, the virion is stabilized between neighboring subunits through carboxyl groups E95 and E97 in close proximity to a Ca(2+) binding site that is shared between two subunits. Upon increase in pH and lower Ca(2+) levels, mutual repulsion of the E95/E97 pair and Ca(2+) removal destabilize the network of interactions between adjacent subunits at lower radius and release the switch for viral disassembly.
Elucidation of the viral disassembly switch of tobacco mosaic virus.,Weis F, Beckers M, von der Hocht I, Sachse C EMBO Rep. 2019 Nov 5;20(11):e48451. doi: 10.15252/embr.201948451. Epub 2019 Sep, 19. PMID:31535454[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weis F, Beckers M, von der Hocht I, Sachse C. Elucidation of the viral disassembly switch of tobacco mosaic virus. EMBO Rep. 2019 Nov 5;20(11):e48451. doi: 10.15252/embr.201948451. Epub 2019 Sep, 19. PMID:31535454 doi:http://dx.doi.org/10.15252/embr.201948451
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