2vq0
From Proteopedia
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- | [[Image:2vq0.png|left|200px]] | ||
- | < | + | ==Capsid structure of Sesbania mosaic virus coat protein deletion mutant rCP(delta 48 to 59)== |
- | + | <StructureSection load='2vq0' size='340' side='right'caption='[[2vq0]], [[Resolution|resolution]] 3.60Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2vq0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sesbania_mosaic_virus Sesbania mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQ0 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6Å</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></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=2vq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vq0 OCA], [https://pdbe.org/2vq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vq0 RCSB], [https://www.ebi.ac.uk/pdbsum/2vq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vq0 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q9EB06_9VIRU Q9EB06_9VIRU] | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vq/2vq0_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </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/main_output.php?pdb_ID=2vq0 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | A unique feature of several T=3 icosahedral viruses is the presence of a structure called the beta-annulus formed by extensive hydrogen bonding between protein subunits related by icosahedral three-fold axis of symmetry. This unique structure has been suggested as a molecular switch that determines the T=3 capsid assembly. In order to examine the importance of the beta-annulus, a deletion mutant of Sesbania mosaic virus coat protein in which residues 48-59 involved in the formation of the beta-annulus were deleted retaining the rest of the residues in the amino terminal segment (rCP (Delta48-59)) was constructed. When expressed in Escherichia coli, the mutant protein assembled into virus like particles of sizes close to that of the wild type virus particles. The purified capsids were crystallized and their three dimensional structure was determined at 3.6 A resolution by X-ray crystallography. The mutant capsid structure closely resembled that of the native virus particles. However, surprisingly, the structure revealed that the assembly of the particles has proceeded without the formation of the beta-annulus. Therefore, the beta-annulus is not essential for T=3 capsid assembly as speculated earlier and may be formed as a consequence of the particle assembly. This is the first structural demonstration that the virus particle morphology with and without the beta-annulus could be closely similar. | ||
- | + | Structure of recombinant capsids formed by the beta-annulus deletion mutant -- rCP (Delta48-59) of Sesbania mosaic virus.,Pappachan A, Subashchandrabose C, Satheshkumar PS, Savithri HS, Murthy MR Virology. 2008 May 25;375(1):190-6. Epub 2008 Mar 4. PMID:18295296<ref>PMID:18295296</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2vq0" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
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[[Category: Sesbania mosaic virus]] | [[Category: Sesbania mosaic virus]] | ||
- | [[Category: | + | [[Category: Anju P]] |
- | [[Category: | + | [[Category: Murthy MRN]] |
- | [[Category: | + | [[Category: Satheshkumar PS]] |
+ | [[Category: Savithri HS]] | ||
+ | [[Category: Subashchandrabose C]] |
Current revision
Capsid structure of Sesbania mosaic virus coat protein deletion mutant rCP(delta 48 to 59)
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