Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1

J Virol. 2004 Nov;78(22):12668-71. doi: 10.1128/JVI.78.22.12668-12671.2004.

Abstract

By electron microscopy and image analysis, we find that baculovirus-expressed UL6 is polymorphic, consisting of rings of 11-, 12-, 13-, and 14-fold symmetry. The 12-mer is likely to be the oligomer incorporated into procapsids: at a resolution of 16 A, it has an axial channel, peripheral flanges, and fits snugly into a vacant vertex site. Its architecture resembles those of bacteriophage portal/connector proteins.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Capsid Proteins / chemistry*
  • Imaging, Three-Dimensional
  • Microscopy, Electron
  • Polymorphism, Genetic
  • Viral Proteins

Substances

  • Capsid Proteins
  • Viral Proteins
  • DNA cleavage and packaging proteins, Herpesvirus