Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus.
The three-dimensional structure of rice dwarf virus was determined to 6.8 A resolution by single particle electron cryomicroscopy. By integrating the structural analysis with bioinformatics, the folds of the proteins in the double-shelled capsid were derived. In the outer shell protein, the uniquely orientated upper and lower domains are composed of similar secondary structure elements but have different relative orientations from that of bluetongue virus in the same Reoviridae family. Differences in both sequence and structure between these proteins may be important in defining virus-host interactions. The inner shell protein adopts a conformation similar to other members of Reoviridae, suggesting a common ancestor that has evolved to infect hosts ranging from plants to animals. Symmetry mismatch between the two shells results in nonequivalent, yet specific, interactions that contribute to the stability of this large macromolecular machine.
Zhou
Z H
ZH
Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030, USA.
Baker
M L
ML
Jiang
W
W
Dougherty
M
M
Jakana
J
J
Dong
G
G
Lu
G
G
Chiu
W
W
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry; D019295:Computational Biology; D008854:Microscopy, Electron / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012087:Reoviridae / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000737:chemistry*
D014764:Viral Proteins