Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse




Journal Article

Tricorn protease exists as an icosahedral supermolecule in vivo

There are no MPG-Authors available
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available

Walz, J., Tamura, T., Tamura, N., Grimm, R., Baumeister, W., & Koster, A. J. (1997). Tricorn protease exists as an icosahedral supermolecule in vivo. Molecular Cell, 1(1), 59-65.

Cite as:
Tricorn protease is the core enzyme of a recently discovered modular proteolytic system. We present evidence that tricorn protease exists in vivo in the form of a higher-order assembly, namely as an icosahedral capsid. Its size exceeds that of many virus particles and represents by far the largest known homooligomeric enzyme complex. Each capsid is built from 20 copies of the tricorn hexameric toroid and thus has a molecular weight of 14.6 MDa. Three-dimensional reconstructions of ice-embedded capsids from electron micrographs show that it is hollow and has large void volumes in its wall. We suggest that the tricorn capsid, in addition to its intrinsic proteolytic activity, serves as the organizing center of a multienzyme complex. [References: 24]