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| | <StructureSection load='1opo' size='340' side='right'caption='[[1opo]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='1opo' size='340' side='right'caption='[[1opo]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1opo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Carnation_mottle_virus Carnation mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OPO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1opo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Carnation_mottle_virus Carnation mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPO FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2tbv|2tbv]]</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=SO4:SULFATE+ION'>SO4</scene></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=1opo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opo OCA], [http://pdbe.org/1opo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1opo RCSB], [http://www.ebi.ac.uk/pdbsum/1opo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1opo 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=1opo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opo OCA], [https://pdbe.org/1opo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opo RCSB], [https://www.ebi.ac.uk/pdbsum/1opo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSD_CARMV CAPSD_CARMV]] Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. Also acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (By similarity). | + | [https://www.uniprot.org/uniprot/CAPSD_CARMV CAPSD_CARMV] Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. Also acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Virus coat protein|Virus coat protein]] | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Carnation mottle virus]] | | [[Category: Carnation mottle virus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dauter, Z]] | + | [[Category: Dauter Z]] |
| - | [[Category: Fry, E]] | + | [[Category: Fry E]] |
| - | [[Category: Mikhailov, A M]] | + | [[Category: Mikhailov AM]] |
| - | [[Category: Morgunova, E]] | + | [[Category: Morgunova E]] |
| - | [[Category: Stuart, D]] | + | [[Category: Stel'mashchuk V]] |
| - | [[Category: Vainshtein, B K]]
| + | [[Category: Stuart D]] |
| - | [[Category: Wilson, K S]]
| + | [[Category: Vainshtein BK]] |
| - | [[Category: Mashchuk, V Stel]]
| + | [[Category: Wilson KS]] |
| - | [[Category: Carmovirus]] | + | |
| - | [[Category: Icosahedral virus]] | + | |
| - | [[Category: Plant virus]] | + | |
| - | [[Category: Tomato bushy stunt virus]]
| + | |
| - | [[Category: Virus]]
| + | |
| - | [[Category: Virus/viral protein]]
| + | |
| Structural highlights
Function
CAPSD_CARMV Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. Also acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the Carnation Mottle Virus (CMtV) capsid protein has been determined at 3.2 A resolution by the method of molecular replacement. Three-dimensional data were collected from a small number of crystals (sp.g. I23, a = 382.6 A) using the synchrotron radiation with an image plate as detector. The coordinates of Tomato Bushy Stunt Virus (TBSV) were used as a searching model. Refinement of the coordinates of 7,479 non-hydrogen atoms performed by the program XPLOR, has led to an R-factor of 18.3%. It was found that the amino acid chain fold of capsid protein is very similar to that in other icosahedral viruses. However, there are some differences in the contact regions between protein subunits and also the lack of the beta-annulus around the 3-fold icosahedral axes. The structural and biochemical results lead us to consider an alternative assembly pathway.
The atomic structure of Carnation Mottle Virus capsid protein.,Morgunova EYu, Dauter Z, Fry E, Stuart DI, Stel'mashchuk VYa, Mikhailov AM, Wilson KS, Vainshtein BK FEBS Lett. 1994 Feb 7;338(3):267-71. PMID:8307192[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morgunova EYu, Dauter Z, Fry E, Stuart DI, Stel'mashchuk VYa, Mikhailov AM, Wilson KS, Vainshtein BK. The atomic structure of Carnation Mottle Virus capsid protein. FEBS Lett. 1994 Feb 7;338(3):267-71. PMID:8307192
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