1vtm: Difference between revisions
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<StructureSection load='1vtm' size='340' side='right' caption='[[1vtm]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1vtm' size='340' side='right' caption='[[1vtm]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vtm]] is a 2 chain structure | <table><tr><td colspan='2'>[[1vtm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VTM FirstGlance]. <br> | ||
</td></tr> | </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=1vtm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vtm OCA], [http://pdbe.org/1vtm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vtm RCSB], [http://www.ebi.ac.uk/pdbsum/1vtm 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=1vtm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vtm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vtm RCSB], [http://www.ebi.ac.uk/pdbsum/1vtm PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://www.uniprot.org/uniprot/CAPSD_TMGMV CAPSD_TMGMV]] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1vtm" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Pattanayek, R]] | [[Category: Pattanayek, R]] | ||
[[Category: Stubbs, G]] | [[Category: Stubbs, G]] | ||
Revision as of 18:07, 10 September 2015
STRUCTURE OF THE U2 STRAIN OF TOBACCO MOSAIC VIRUS REFINED AT 3.5 ANGSTROMS RESOLUTION USING X-RAY FIBER DIFFRACTIONSTRUCTURE OF THE U2 STRAIN OF TOBACCO MOSAIC VIRUS REFINED AT 3.5 ANGSTROMS RESOLUTION USING X-RAY FIBER DIFFRACTION
Structural highlights
Function[CAPSD_TMGMV] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. 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 PubMedThe structure of the U2 strain of tobacco mosaic virus (TMV) has been determined by fiber diffraction methods at 3.5 A resolution, and refined by a combination of restrained least-squares and molecular dynamics methods to an R-factor of 0.096. The structure is extremely similar to that of the common strain of TMV, with the largest differences being in the protein loop that makes up the inner surface of the virus, and in the C-terminal region on the outer surface. Differences in the inner loop can be correlated with differences in the properties of the two viruses. Structure of the U2 strain of tobacco mosaic virus refined at 3.5 A resolution using X-ray fiber diffraction.,Pattanayek R, Stubbs G J Mol Biol. 1992 Nov 20;228(2):516-28. PMID:1453461[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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