Capsids of tricorn protease studied by electron cryomicroscopy.
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.
Walz
J
J
Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Martinsried, 82152, Germany.
Koster
A J
AJ
Tamura
T
T
Baumeister
W
W
D019843:Archaeal Proteins / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D003546:Cysteine Endopeptidases / Q000378:metabolism; D010450:Endopeptidases / Q000648:ultrastructure*; D005583:Fourier Analysis; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D013822:Thermoplasma
D019843:Archaeal Proteins; D009097:Multienzyme Complexes; D010450:Endopeptidases; C102094:tricorn protease; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex