1TMF

THREE-DIMENSIONAL STRUCTURE OF THEILER MURINE ENCEPHALOMYELITIS VIRUS (BEAN STRAIN)

Summary for 1TMF

• Entry DOI: 10.2210/pdb1tmf/pdb
• Descriptor: THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP1), THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP2), THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP3), ... (4 entities in total)
• Functional Keywords: coat protein, icosahedral virus, virus
• Biological source: Theiler's encephalomyelitis virus; 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): P08544 P08544 P08544 P13899
• Total number of polymer chains: 4
• Total formula weight: 90264.76

Authors

Luo, M.,Toth, K.S. (deposition date: 1992-02-20, release date: 1993-10-31, Last modification date: 2023-04-19)

Primary citation

Luo, M.,He, C.,Toth, K.S.,Zhang, C.X.,Lipton, H.L.
Three-dimensional structure of Theiler murine encephalomyelitis virus (BeAn strain).
Proc.Natl.Acad.Sci.USA, 89:2409-2413, 1992

PubMed Abstract: Depending on the strain, Theiler murine encephalomyelitis virus (TMEV) may cause acute encephalitis or chronic demyelinating disease, which is associated with viral persistence in mice. Persistent central nervous system infection and demyelination by the less-virulent TMEV has provided a useful animal model for the human demyelinating disease multiple sclerosis. The less-virulent BeAn strain of TMEV was crystallized and its atomic structure was determined by x-ray crystallography. The alpha-carbon coordinates of the closely related Mengo virus were used to calculate the initial phases to 3.5 A resolution and the interpretable electron density map was produced by 10 cycles of 30-fold noncrystallographic molecular replacement averaging. The structure revealed a high degree of overall structural similarity to Mengo virus as well as substantial differences in the surface loops. These structural changes might be correlated with TMEV host-specific recognition, pH-related stability, and neurovirulence.

PubMed: 1312722
DOI: 10.1073/pnas.89.6.2409

Experimental method

X-RAY DIFFRACTION (3.5 Å)