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Capsids of tricorn protease studied by electron cryomicroscopy
1Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Martinsried, 82152, Germany.
Journal of Structural Biology
|December 22, 1999
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.