This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1cov
From Proteopedia
(New page: 200px<br /><applet load="1cov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cov, resolution 3.50Å" /> '''COXSACKIEVIRUS B3 CO...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1cov.gif|left|200px]]<br /><applet load="1cov" size=" | + | [[Image:1cov.gif|left|200px]]<br /><applet load="1cov" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cov, resolution 3.50Å" /> | caption="1cov, resolution 3.50Å" /> | ||
'''COXSACKIEVIRUS B3 COAT PROTEIN'''<br /> | '''COXSACKIEVIRUS B3 COAT PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of coxsackievirus B3 (CVB3) has been determined to | + | The crystal structure of coxsackievirus B3 (CVB3) has been determined to 3.5 A resolution. The icosahedral CVB3 particles crystallize in the monoclinic space group, P2(1), (a = 574.6, b = 302.1, c = 521.6 A, beta = 107.7 degrees ) with two virions in the asymmetric unit giving 120-fold non-crystallographic redundancy. The crystals diffracted to 2.7 A resolution and the X-ray data set was 55% complete to 3.0,4, resolution. Systematically weak reflections and the self-rotation function established pseudo R32 symmetry with each particle sitting on a 32 special position. This constrained the orientation and position of each particle in the monoclinic cell to near face-centered positions and allowed for a total of six possible monoclinic space-group settings. Correct interpretation of the high-resolution (3.0-3.2 A) self-rotation function was instrumental in determining the deviations from R32 orientations of the virus particles in the unit cell. Accurate particle orientations permitted the correct assignment of the crystal space-group setting amongst the six ambiguous possibilities and for the correct determination of particle positions. Real-space electron-density averaging and phase refinement, using human rhinovius 14 (HRV14) as an initial phasing model, have been carried out to 3.5 A resolution. The initial structural model has been built and refined to 3.5 A resolution using X-PLOR. |
==About this Structure== | ==About this Structure== | ||
| - | 1COV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_coxsackievirus_b1 Human coxsackievirus b1] with MYR and PLM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1COV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_coxsackievirus_b1 Human coxsackievirus b1] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=PLM:'>PLM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COV OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Human coxsackievirus b1]] | [[Category: Human coxsackievirus b1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Muckelbauer, J | + | [[Category: Muckelbauer, J K.]] |
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
[[Category: MYR]] | [[Category: MYR]] | ||
[[Category: PLM]] | [[Category: PLM]] | ||
| Line 20: | Line 20: | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:10 2008'' |
Revision as of 10:08, 21 February 2008
|
COXSACKIEVIRUS B3 COAT PROTEIN
Overview
The crystal structure of coxsackievirus B3 (CVB3) has been determined to 3.5 A resolution. The icosahedral CVB3 particles crystallize in the monoclinic space group, P2(1), (a = 574.6, b = 302.1, c = 521.6 A, beta = 107.7 degrees ) with two virions in the asymmetric unit giving 120-fold non-crystallographic redundancy. The crystals diffracted to 2.7 A resolution and the X-ray data set was 55% complete to 3.0,4, resolution. Systematically weak reflections and the self-rotation function established pseudo R32 symmetry with each particle sitting on a 32 special position. This constrained the orientation and position of each particle in the monoclinic cell to near face-centered positions and allowed for a total of six possible monoclinic space-group settings. Correct interpretation of the high-resolution (3.0-3.2 A) self-rotation function was instrumental in determining the deviations from R32 orientations of the virus particles in the unit cell. Accurate particle orientations permitted the correct assignment of the crystal space-group setting amongst the six ambiguous possibilities and for the correct determination of particle positions. Real-space electron-density averaging and phase refinement, using human rhinovius 14 (HRV14) as an initial phasing model, have been carried out to 3.5 A resolution. The initial structural model has been built and refined to 3.5 A resolution using X-PLOR.
About this Structure
1COV is a Single protein structure of sequence from Human coxsackievirus b1 with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure determination of coxsackievirus B3 to 3.5 A resolution., Muckelbauer JK, Kremer M, Minor I, Tong L, Zlotnick A, Johnson JE, Rossmann MG, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):871-87. PMID:15299757
Page seeded by OCA on Thu Feb 21 12:08:10 2008
