Protein-RNA interactions in an icosahedral virus at 3.0 A resolution.
Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV) binds to the capsid interior in a symmetric fashion and is clearly visible in the electron density map. The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereochemical properties. Interactions with protein are dominated by nonbonding forces with few specific contacts. The tertiary and quaternary structures of the BPMV capsid proteins are similar to those observed in animal picornaviruses, supporting the close relation between plant comoviruses and animal picornaviruses established by previous biological studies.
Chen
Z G
ZG
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.
Stauffacher
C
C
Li
Y
Y
Schmidt
T
T
Bomu
W
W
Kamer
G
G
Shanks
M
M
Lomonossoff
G
G
Johnson
J E
JE
D000595:Amino Acid Sequence; D002213:Capsid / Q000378:metabolism* / Q000648:ultrastructure; D003461:Crystallography; D004577:Electron Probe Microanalysis; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009029:Mosaic Viruses / Q000032:analysis* / Q000235:genetics / Q000648:ultrastructure; D010942:Plant Viruses / Q000032:analysis* / Q000235:genetics / Q000648:ultrastructure; D011487:Protein Conformation; D012367:RNA, Viral / Q000378:metabolism* / Q000648:ultrastructure
D046911:Macromolecular Substances; D012367:RNA, Viral