1e57
From Proteopedia
(New page: 200px<br /><applet load="1e57" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e57, resolution 3.2Å" /> '''PHYSALIS MOTTLE VIRUS...) |
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| - | [[Image:1e57.gif|left|200px]]<br /><applet load="1e57" size=" | + | [[Image:1e57.gif|left|200px]]<br /><applet load="1e57" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e57, resolution 3.2Å" /> | caption="1e57, resolution 3.2Å" /> | ||
'''PHYSALIS MOTTLE VIRUS: EMPTY CAPSID'''<br /> | '''PHYSALIS MOTTLE VIRUS: EMPTY CAPSID'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional crystal structure of the empty capsid of Physalis | + | 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== | ==About this Structure== | ||
| - | 1E57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physalis_mottle_virus Physalis mottle virus]. Full crystallographic information is available from [http:// | + | 1E57 is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
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[[Category: Physalis mottle virus]] | [[Category: Physalis mottle virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Krishna, S | + | [[Category: Krishna, S S.]] |
| - | [[Category: Murthy, M | + | [[Category: Murthy, M R.N.]] |
[[Category: Sastri, M.]] | [[Category: Sastri, M.]] | ||
| - | [[Category: Savithri, H | + | [[Category: Savithri, H S.]] |
[[Category: coat protein (viral)]] | [[Category: coat protein (viral)]] | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:57 2008'' |
Revision as of 10:23, 21 February 2008
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PHYSALIS MOTTLE VIRUS: EMPTY CAPSID
Overview
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
1E57 is a Single protein structure of sequence from Physalis mottle virus. Full crystallographic information is available from OCA.
Reference
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
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