Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Tricorn protease - the core of a modular proteolytic system

There are no MPG-Authors in the publication available
External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Tamura, T., Tamura, N., Cejka, Z., Hegerl, R., Lottspeich, F., & Baumeister, W. (1996). Tricorn protease - the core of a modular proteolytic system. Science, 274(5291), 1385-1389.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-72CE-E
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. [References: 31]