1ng0: Difference between revisions
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==The three-dimensional structure of Cocksfoot mottle virus at 2.7A resolution== | ==The three-dimensional structure of Cocksfoot mottle virus at 2.7A resolution== | ||
<StructureSection load='1ng0' size='340' side='right' caption='[[1ng0]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1ng0' size='340' side='right' caption='[[1ng0]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2n|1f2n]], [[1sbv|1sbv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2n|1f2n]], [[1sbv|1sbv]]</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=1ng0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ng0 OCA], [http://pdbe.org/1ng0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ng0 RCSB], [http://www.ebi.ac.uk/pdbsum/1ng0 PDBsum]</span></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=1ng0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ng0 OCA], [http://pdbe.org/1ng0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ng0 RCSB], [http://www.ebi.ac.uk/pdbsum/1ng0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ng0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=1ng0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 13:16, 25 October 2017
The three-dimensional structure of Cocksfoot mottle virus at 2.7A resolutionThe three-dimensional structure of Cocksfoot mottle virus at 2.7A resolution
Structural highlights
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 PubMedCocksfoot mottle virus is a plant virus that belongs to the genus Sobemovirus. The structure of the virus has been determined at 2.7 A resolution. The icosahedral capsid has T = 3 quasisymmetry and 180 copies of the coat protein. Except for a couple of stacked bases, the viral RNA is not visible in the electron density map. The coat protein has a jelly-roll beta-sandwich fold and its conformation is very similar to that of other sobemoviruses and tobacco necrosis virus. The N-terminal arm of one of the three quasiequivalent subunits is partly ordered and follows the same path in the capsid as the arm in rice yellow mottle virus, another sobemovirus. In other sobemoviruses, the ordered arm follows a different path, but in both cases the arms from three subunits meet and form a similar structure at a threefold axis. A comparison of the structures and sequences of viruses in this family shows that the only conserved parts of the protein-protein interfaces are those that form binding sites for calcium ions. Still, the relative orientations and position of the subunits are maintained. The three-dimensional structure of cocksfoot mottle virus at 2.7 A resolution.,Tars K, Zeltins A, Liljas L Virology. 2003 Jun 5;310(2):287-97. PMID:12781716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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