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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



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ID: 318490.0, MPI für Biochemie / Structural Biology (W. Baumeister)
The proteasome - a macromolecular assembly designed to confine proteolysis to a nanocompartment
Authors:Baumeister, W.; Cejka, Z.; Kania, M.; Seemüller, E.
Date of Publication (YYYY-MM-DD):1997
Title of Journal:Biological Chemistry
Volume:378
Issue / Number:3-4
Start Page:121
End Page:130
Review Status:not specified
Audience:Not Specified
Abstract / Description:Significant progress has been made over the past few years in elucidating the structural principles and the enzymatic mechanism of the 20S proteasome. As a result, the proteasome has become the prototype of a new family of enzymes, the Ntn hydrolases, as well as a paradigm for macromolecular assemblies that confine their proteolytic activity to an inner nanocompartment. Since access to this nanocompartment is restricted to unfolded substrate polypeptides, the 20S proteasome must be functionally linked to a substrate recognition and unfolding machinery. In eukaryotes this is provided by the 19S 'cap' complex, which associates with the 20S core to form the 26S proteasome, a protease capable of degrading ubiquitinated proteins in an ATP-dependent manner. [References: 88]
Free Keywords:Atp-dependent proteolysis; Macromolecular; Assembly; Ntn hydrolases; 20s/26s proteasome; Protein degradation; Ubiquitin-pathway.; Multicatalytic proteinase complex; Peptide-hydrolyzing activity; Molecular-weight protease; Thermoplasma-acidophilum; Escherichia-coli; Yeast proteasome; 20s proteasome; 3-dimensional structure; Electron-microscopy; Prosome particle.; Biochemistry & biophysics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)
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