1e57: Difference between revisions

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[[Image:1e57.gif|left|200px]]
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{{STRUCTURE_1e57|  PDB=1e57  |  SCENE=  }}
'''PHYSALIS MOTTLE VIRUS: EMPTY CAPSID'''


==PHYSALIS MOTTLE VIRUS: EMPTY CAPSID==
<StructureSection load='1e57' size='340' side='right'caption='[[1e57]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e57]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Physalis_mottle_virus Physalis mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E57 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]] 3.2&#8491;</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=1e57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e57 OCA], [https://pdbe.org/1e57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e57 RCSB], [https://www.ebi.ac.uk/pdbsum/1e57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e57 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COAT_PHMV COAT_PHMV]
== 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/e5/1e57_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1e57 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional crystal structure of the empty capsid of Physalis mottle tymovirus has been determined to 3.2 A resolution. The empty capsids crystallized in the space group P1, leading to 60-fold non-crystallographic redundancy. The known structure of Physalis mottle virus was used as a phasing model to initiate the structure determination by real-space electron-density averaging. The main differences between the structures of the native and the empty capsids were in residues 10 to 28 of the A-subunit, residues 1 to 9 of the B-subunit and residues 1 to 5 of the C-subunit, which are ordered only in the native virus particles. An analysis of the subunit disposition reveals that the virus has expanded radially outward by approximately 1.8 A in the empty particles. The A-subunits move in a direction that makes 10 degrees to the icosahedral 5-fold axes of symmetry. The B and C-subunits move along vectors making 12 degrees and 15 degrees to the quasi 6-fold axes. The quaternary organization of the pentameric and hexameric capsomeres are not altered significantly. However, the pentamer-hexamer contacts are reduced. Therefore, encapsidation of RNA appears to cause a reduction in the particle radius concomittant with the ordering of the N-terminal arm in the three subunits. These structural changes in Physalis mottle virus appear to be larger than the corresponding changes observed in viruses for which both the empty and full particle structures have been determined.


==Overview==
Structural studies on the empty capsids of Physalis mottle virus.,Krishna SS, Sastri M, Savithri HS, Murthy MR J Mol Biol. 2001 Apr 6;307(4):1035-47. PMID:11286554<ref>PMID:11286554</ref>
The three-dimensional crystal structure of the empty capsid of Physalis mottle tymovirus has been determined to 3.2 A resolution. The empty capsids crystallized in the space group P1, leading to 60-fold non-crystallographic redundancy. The known structure of Physalis mottle virus was used as a phasing model to initiate the structure determination by real-space electron-density averaging. The main differences between the structures of the native and the empty capsids were in residues 10 to 28 of the A-subunit, residues 1 to 9 of the B-subunit and residues 1 to 5 of the C-subunit, which are ordered only in the native virus particles. An analysis of the subunit disposition reveals that the virus has expanded radially outward by approximately 1.8 A in the empty particles. The A-subunits move in a direction that makes 10 degrees to the icosahedral 5-fold axes of symmetry. The B and C-subunits move along vectors making 12 degrees and 15 degrees to the quasi 6-fold axes. The quaternary organization of the pentameric and hexameric capsomeres are not altered significantly. However, the pentamer-hexamer contacts are reduced. Therefore, encapsidation of RNA appears to cause a reduction in the particle radius concomittant with the ordering of the N-terminal arm in the three subunits. These structural changes in Physalis mottle virus appear to be larger than the corresponding changes observed in viruses for which both the empty and full particle structures have been determined.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1E57 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physalis_mottle_virus Physalis mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E57 OCA].
</div>
<div class="pdbe-citations 1e57" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural studies on the empty capsids of Physalis mottle virus., Krishna SS, Sastri M, Savithri HS, Murthy MR, J Mol Biol. 2001 Apr 6;307(4):1035-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11286554 11286554]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physalis mottle virus]]
[[Category: Physalis mottle virus]]
[[Category: Single protein]]
[[Category: Krishna SS]]
[[Category: Krishna, S S.]]
[[Category: Murthy MRN]]
[[Category: Murthy, M R.N.]]
[[Category: Sastri M]]
[[Category: Sastri, M.]]
[[Category: Savithri HS]]
[[Category: Savithri, H S.]]
[[Category: Icosahedral virus]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:40:30 2008''

Latest revision as of 11:52, 13 December 2023

PHYSALIS MOTTLE VIRUS: EMPTY CAPSID

1e57, resolution 3.20Å

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