Capsids of tricorn protease studied by electron cryomicroscopy

J Struct Biol. 1999 Dec 1;128(1):65-8. doi: 10.1006/jsbi.1999.4169.

Abstract

Tricorn protease from the archaeon Thermoplasma acidophilum acts "downstream" of the proteasome; in conjunction with its aminopeptidase cofactors it converts peptides generated by the proteasome into free amino acids. The basic functional unit of Tricorn is a homohexamer of the 121-kDa subunit, 20 of which can assemble further to form an icosahedral capsid with a molecular mass of 14.6 MDa. We have used electron cryomicroscopy to determine the structure of the Tricorn capsids to a resolution of 1.3 nm.

MeSH terms

  • Archaeal Proteins / ultrastructure*
  • Cryoelectron Microscopy*
  • Cysteine Endopeptidases / metabolism
  • Endopeptidases / ultrastructure*
  • Fourier Analysis
  • Image Processing, Computer-Assisted
  • Models, Molecular
  • Multienzyme Complexes / metabolism
  • Proteasome Endopeptidase Complex
  • Protein Conformation
  • Thermoplasma

Substances

  • Archaeal Proteins
  • Multienzyme Complexes
  • Endopeptidases
  • tricorn protease
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex