Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage phi29 connector particle

J Mol Biol. 1998 Aug 14;281(2):219-25. doi: 10.1006/jmbi.1998.1928.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus Phages / chemistry*
  • Capsid / chemistry*
  • Capsid / ultrastructure
  • Capsid Proteins*
  • Crystallization
  • Crystallography, X-Ray / methods*
  • Image Processing, Computer-Assisted
  • Microscopy, Electron

Substances

  • Capsid Proteins
  • portal protein, bacteriophage phi29