Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system.
The satellite bacteriophage P4 does not have genes coding for any major structural proteins, but assembles a capsid from the gene products of bacteriophage P2. The capsid assembled under control of P4 is smaller (45 nm) than the normal P2 capsid (60 nm). The low resolution (4.5 nm) structures of P2 and P4 capsids were determined by cryo-electron microscopy and image processing. The capsid of P2 shows T = 7 symmetry with most of the mass clustered as 12 pentamers and 60 hexamers. The P4 capsid has T = 4 symmetry with a similar distribution of mass to P2, but the hexamer geometry has changed. The major capsid protein has a two-domain structure. The major domains form the capsomers proper, while connecting domains form trivalent contacts between the capsomers. The size determination by P4 appears to function by altering hexamer geometry rather than by affecting the interdomain angle alone.
Dokland
T
T
European Molecular Biology Laboratory, Biological Structures and Biocomputing Programme, Heidelberg, Germany.
Lindqvist
B H
BH
Fuller
S D
SD
D001435:Bacteriophages / Q000648:ultrastructure*; D002213:Capsid / Q000648:ultrastructure; D003080:Cold Temperature; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron / Q000379:methods