Tricorn protease--the core of a modular proteolytic system.
Large macromolecular assemblies have evolved as a means of compartmentalizing reactions in organisms lacking membrane-bounded compartments. A tricorn-shaped protease was isolated from the archaeon Thermoplasma and was shown to form a multisubunit proteolytic complex. The 120-kilodalton monomer assembled to form a hexameric toroid that could assemble further into a capsid structure. Tricorn protease appeared to act as the core of a proteolytic system; when it interacted with several smaller proteins, it displayed multicatalytic activities.
Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany.
T
T
Tamura
N
N
Tamura
Z
Z
Cejka
R
R
Hegerl
F
F
Lottspeich
W
W
Baumeister
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000378:metabolism; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D005798:Genes, Bacterial; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D013822:Thermoplasma / Q000201:enzymology*
D009097:Multienzyme Complexes; D010455:Peptides; D011994:Recombinant Proteins; D010450:Endopeptidases; C102094:tricorn protease; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex