Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage phi29 connector particle.
The internal symmetry of the connector or portal particle from the double-stranded DNA bacteriophage phi29 has been examined by X-ray crystallography. This large multimeric structure (420 kDa) is built up by a number of identical subunits of the p10 protein. It connects the head of the virus with the tail and plays a central role in the prohead assembly and DNA packaging. For the first time a bacteriophage connector has been crystallized and X-ray data have been collected up to a resolution of 3.2 A. A self-rotation function has been calculated, unambigously revealing the 12-fold symmetry of the particle and its orientation in the crystal lattice. The orientation has been confirmed by calculating a cross-rotation function using a low resolution model based on electron microscopy reconstructions.
Guasch
A
A
Departament de Biologia Molecular i Cel.lular, Centre d'Investigació i Desenvolupament, CSIC, Jordi Girona, Barcelona, 18-26 08034, Spain.
Pous
J
J
Párraga
A
A
Valpuesta
J M
JM
Carrascosa
J L
JL
Coll
M
M
D017103:Bacillus Phages / Q000737:chemistry*; D002213:Capsid / Q000737:chemistry* / Q000648:ultrastructure; D036022:Capsid Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron
D036022:Capsid Proteins; C097975:portal protein, bacteriophage phi29