1EV1

ECHOVIRUS 1

Summary for 1EV1

• Entry DOI: 10.2210/pdb1ev1/pdb
• Descriptor: ECHOVIRUS 1, PALMITIC ACID, MYRISTIC ACID, ... (7 entities in total)
• Functional Keywords: viral coat protein, capsid, picornavirus, echovirus, icosahedral virus, virus
• Biological source: Human echovirus 1; 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): O91734 O91734 O91734 O91734
• Total number of polymer chains: 4
• Total formula weight: 94084.84

Authors

Wien, M.W.,Filman, D.J.,Hogle, J.M. (deposition date: 1997-12-02, release date: 1999-01-27, Last modification date: 2024-11-13)

Primary citation

Filman, D.J.,Wien, M.W.,Cunningham, J.A.,Bergelson, J.M.,Hogle, J.M.
Structure determination of echovirus 1.
Acta Crystallogr.,Sect.D, 54:1261-1272, 1998

PubMed Abstract: The atomic structure of echovirus 1 (a member of the enterovirus genus of the picornavirus family) has been determined using cryo-crystallography and refined to 3.55 A resolution. Echovirus 1 crystallizes in space group P22121 with a = 352.45, b = 472.15 and c = 483.20 A. The crystals contain one full virus particle in the asymmetric unit allowing for 60-fold noncrystallographic symmetry averaging. The diffraction pattern shows strong pseudo-B-centering with reflections with h + l = 2n + 1 being systematically weak or absent below about 6 A resolution. The size of the unit cell and presence of pseudo-B-centering placed strong constraints on the allowed packing of the icosahedral particle in the crystal lattice. These constraints greatly facilitated the determination of the orientation and position of the virus by reducing the dimensionality of the search, but interactions between the crystallographic and noncrystallographic symmetries rendered the choice of space group ambiguous until very late in the structure determination. This structure determination provides a striking example of the power of packing analysis in molecular replacement and illustrates how subtle interactions between crystallographic and noncrystallographic symmetries can be resolved.

PubMed: 10089503
DOI: 10.1107/S0907444998002790

Experimental method

X-RAY DIFFRACTION (3.55 Å)