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Structural basis for the processive protein degradation by tricorn protease

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77801

Brandstetter,  H.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78216

Kim,  J. S.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78033

Groll,  M.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78015

Göttig,  P.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Brandstetter, H., Kim, J. S., Groll, M., Göttig, P., & Huber, R. (2002). Structural basis for the processive protein degradation by tricorn protease. Biological Chemistry, 383(7-8), 1157-1165.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6EDA-8
Abstract
Cell survival critically depends on the efficient use of available resources. This includes both the clearance and the recycling of those protein components that have become futile or defective. Several proteins sequentially accomplish this complex task. The proteasome serves as an initial protein shredder and generates peptides of 7-12 amino acids in length. In general, these products are useless burden to the cell and need further processing. A few years ago, a proteolytic system was identified in the model organism Thermoplasma acidophilum which indeed performs this processing [Tamura et al., Science 274 (1996), 1385 1389]. The hexameric core protein of this modular system, referred to as tricorn protease, is a 720 kDa protease which is able to assemble further into a giant icosahedral capsid, as determined by electron microscopy. Recently, we determined the crystal structure of the tricorn core particle at 2.0 a resolution [Brandstetter et al., Nature 414 (2001), 466 469]. Here we describe the structural and mechanistic basis for tricorns processive degradation mode, including a novel electrostatic substratetoproduct sink, and suggest how further components might interact with the tricorn protease to complete the cellular waste recycling process.