1COV

COXSACKIEVIRUS B3 COAT PROTEIN

Summary for 1COV

• Entry DOI: 10.2210/pdb1cov/pdb
• Descriptor: COXSACKIEVIRUS COAT PROTEIN, PALMITIC ACID, MYRISTIC ACID, ... (6 entities in total)
• Functional Keywords: coxsackievirus b3, icosahedral virus, virus
• Biological source: Human coxsackievirus B3; More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): Q66282 Q66282 Q66282 Q66282
• Total number of polymer chains: 4
• Total formula weight: 94320.20

Authors

Muckelbauer, J.K.,Rossmann, M.G. (deposition date: 1994-10-19, release date: 1996-03-08, Last modification date: 2024-12-25)

Primary citation

Muckelbauer, J.K.,Kremer, M.,Minor, I.,Tong, L.,Zlotnick, A.,Johnson, J.E.,Rossmann, M.G.
Structure determination of coxsackievirus B3 to 3.5 A resolution.
Acta Crystallogr.,Sect.D, 51:871-887, 1995

PubMed Abstract: 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.

PubMed: 15299757
DOI: 10.1107/S0907444995002253

Experimental method

X-RAY DIFFRACTION (3.5 Å)