Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus.
Three-dimensional structures of the empty procapsid and the mature capsid of the Salmonella bacteriophage P22 have been determined to a resolution of 28 A using electron cryomicroscopy and computer image processing. The coat subunits in both the structures are arranged as pentamers and hexamers on a T = 7 icosahedral lattice. The two structures display significant differences in shape, size and intersubunit interactions. The empty procapsid is spherical in contrast to the distinctly larger and polyhedral mature capsid. The empty procapsid structure exhibits holes at all the quasi sixfold positions that are absent in the mature capsid. These holes may be the exit ports for scaffolding subunits. Detailed comparisons of the two structures indicate that extensive structural changes take place during maturation in all seven quasi-equivalent subunits. These changes cause flattening of the icosahedral facets, capsid expansion and closing of the holes. This process results in a stable and impenetrable capsid that protects the bacterial genome.
Prasad
B V
BV
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030.
Prevelige
P E
PE
Marietta
E
E
Chen
R O
RO
Thomas
D
D
King
J
J
Chiu
W
W
D017100:Bacteriophage P22 / Q000235:genetics / Q000378:metabolism*; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D003198:Computer Simulation; D016679:Genome, Viral; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism
D046911:Macromolecular Substances