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| <StructureSection load='1laj' size='340' side='right'caption='[[1laj]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='1laj' size='340' side='right'caption='[[1laj]], [[Resolution|resolution]] 3.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1laj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Tomato_aspermy_virus Tomato aspermy virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1laj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Tomato_aspermy_virus Tomato aspermy virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAJ FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 3.4Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f15|1f15]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1laj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1laj OCA], [http://pdbe.org/1laj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1laj RCSB], [http://www.ebi.ac.uk/pdbsum/1laj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1laj 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=1laj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1laj OCA], [https://pdbe.org/1laj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1laj RCSB], [https://www.ebi.ac.uk/pdbsum/1laj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1laj ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/CAPSD_TAV CAPSD_TAV]] Capsid protein. Probably binds RNA and plays a role in packaging (By similarity). | + | [https://www.uniprot.org/uniprot/CAPSD_TAV CAPSD_TAV] Capsid protein. Probably binds RNA and plays a role in packaging (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: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Tomato aspermy virus]] | | [[Category: Tomato aspermy virus]] |
- | [[Category: Canady, M A]] | + | [[Category: Canady MA]] |
- | [[Category: Larson, S B]] | + | [[Category: Larson SB]] |
- | [[Category: Lucas, R W]] | + | [[Category: Lucas RW]] |
- | [[Category: McPherson, A]] | + | [[Category: McPherson A]] |
- | [[Category: Anti-parallel beta sheet]]
| + | |
- | [[Category: Disulphide bridge]]
| + | |
- | [[Category: Icosahedral virus]]
| + | |
- | [[Category: Jelly roll]]
| + | |
- | [[Category: Protein-rna complex]]
| + | |
- | [[Category: T=3 icosahedral virus]]
| + | |
- | [[Category: Virus-rna complex]]
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| Structural highlights
Function
CAPSD_TAV Capsid protein. Probably binds RNA and plays a role in packaging (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 three-dimensional structure of tomato aspermy virus (TAV) has been solved by X-ray crystallography and refined to an R factor of 0.218 for 3.4-40 A data (effective resolution of 4A). Molecular replacement, using cucumber mosaic virus (Smith et al., 2000), provided phases for the initial maps used for model building. The coat protein of the 280 A diameter virion has the canonical "Swiss roll" beta-barrel topology with a distinctive amino-terminal alpha-helix directed into the interior of the virus where it interacts with encapsidated RNA. The N-terminal helices are joined to the beta-barrels of protein subunits by extended polypeptides of six amino acids, which serve as flexible hinges allowing movement of the helices in response to local RNA distribution. Segments of three nucleotides of partially disordered RNA interact with the capsid, primarily through arginine residues, at interfaces between A and B subunits. Side chains of cys64 and cys106 form the first disulfide observed in a cucumovirus, including a unique cysteine, 106, in a region otherwise conserved. A positive ion, putatively modeled as a Mg(+)ion, lies on the quasi-threefold axis surrounded by three quasi-symmetric glutamate 175 side chains.
The structure of tomato aspermy virus by X-ray crystallography.,Lucas RW, Larson SB, Canady MA, McPherson A J Struct Biol. 2002 Aug;139(2):90-102. PMID:12406691[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lucas RW, Larson SB, Canady MA, McPherson A. The structure of tomato aspermy virus by X-ray crystallography. J Struct Biol. 2002 Aug;139(2):90-102. PMID:12406691
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