Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly.
Three-dimensional structures of the double-stranded DNA bacteriophage phi29 scaffolding protein (gp7) before and after prohead assembly have been determined at resolutions of 2.2 and 2.8 A, respectively. Both structures are dimers that resemble arrows, with a four-helix bundle composing the arrowhead and a coiled coil forming the tail. The structural resemblance of gp7 to the yeast transcription factor GCN4 suggests a DNA-binding function that was confirmed by native gel electrophoresis. DNA binding to gp7 may have a role in mediating the structural transition from prohead to mature virus and scaffold release. A cryo-EM analysis indicates that gp7 is arranged inside the capsid as a series of concentric shells. The position of the higher density features in these shells correlates with the positions of hexamers in the equatorial region of the capsid, suggesting that gp7 may regulate formation of the prolate head through interactions with these hexamers.
Morais
Marc C
MC
Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907-2054, USA.
Kanamaru
Shuji
S
Badasso
Mohammed O
MO
Koti
Jaya S
JS
Owen
Barbara A L
BA
McMurray
Cynthia T
CT
Anderson
Dwight L
DL
Rossmann
Michael G
MG
D017103:Bacillus Phages / Q000737:chemistry*; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
D014764:Viral Proteins; D004247:DNA