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| | <StructureSection load='3zxa' size='340' side='right'caption='[[3zxa]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='3zxa' size='340' side='right'caption='[[3zxa]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zxa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Turnip_crinkle_virus Turnip crinkle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZXA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zxa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Turnip_crinkle_virus Turnip crinkle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZXA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zx8|3zx8]], [[3zx9|3zx9]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zx8|3zx8]], [[3zx9|3zx9]]</div></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=3zxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zxa OCA], [http://pdbe.org/3zxa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zxa RCSB], [http://www.ebi.ac.uk/pdbsum/3zxa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zxa 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=3zxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zxa OCA], [https://pdbe.org/3zxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zxa RCSB], [https://www.ebi.ac.uk/pdbsum/3zxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zxa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSD_TCV CAPSD_TCV]] 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.<ref>PMID:12477856</ref> <ref>PMID:12620795</ref> <ref>PMID:20439431</ref> | + | [[https://www.uniprot.org/uniprot/CAPSD_TCV CAPSD_TCV]] 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.<ref>PMID:12477856</ref> <ref>PMID:12620795</ref> <ref>PMID:20439431</ref> |
| | <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 protein|Virus coat protein]] | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[CAPSD_TCV] 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.[1] [2] [3]
Publication Abstract from PubMed
The structure of turnip crinkle virus has been determined at 3.2 A resolution, using the electron density of tomato bushy stunt virus as a starting point for phase refinement by non-crystallographic symmetry. The structures are very closely related, especially in the subunit arm and S domain, where only small insertions and deletions and small co-ordinate shifts relate one chain to another. The P domains, although quite similar in fold, are oriented somewhat differently with respect to the S domains. Understanding of the structure of turnip crinkle virus has been important for analyzing its assembly, as described in an accompanying paper.
Structure and assembly of turnip crinkle virus. I. X-ray crystallographic structure analysis at 3.2 A resolution.,Hogle JM, Maeda A, Harrison SC J Mol Biol. 1986 Oct 20;191(4):625-38. PMID:3806676[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Qu F, Ren T, Morris TJ. The coat protein of turnip crinkle virus suppresses posttranscriptional gene silencing at an early initiation step. J Virol. 2003 Jan;77(1):511-22. PMID:12477856
- ↑ Thomas CL, Leh V, Lederer C, Maule AJ. Turnip crinkle virus coat protein mediates suppression of RNA silencing in Nicotiana benthamiana. Virology. 2003 Feb 1;306(1):33-41. PMID:12620795
- ↑ Azevedo J, Garcia D, Pontier D, Ohnesorge S, Yu A, Garcia S, Braun L, Bergdoll M, Hakimi MA, Lagrange T, Voinnet O. Argonaute quenching and global changes in Dicer homeostasis caused by a pathogen-encoded GW repeat protein. Genes Dev. 2010 May;24(9):904-15. doi: 10.1101/gad.1908710. PMID:20439431 doi:http://dx.doi.org/10.1101/gad.1908710
- ↑ Hogle JM, Maeda A, Harrison SC. Structure and assembly of turnip crinkle virus. I. X-ray crystallographic structure analysis at 3.2 A resolution. J Mol Biol. 1986 Oct 20;191(4):625-38. PMID:3806676
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