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



ID: 318686.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Tricorn protease exists as an icosahedral supermolecule in vivo
Authors:Walz, J.; Tamura, T.; Tamura, N.; Grimm, R.; Baumeister, W.; Koster, A. J.
Date of Publication (YYYY-MM-DD):1997-12
Title of Journal:Molecular Cell
Volume:1
Issue / Number:1
Start Page:59
End Page:65
Audience:Not Specified
Abstract / Description: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]
Free Keywords:Automatic electron tomography; Crystal-structure; Cryoelectron microscopy; 3-dimensional structure; Riboflavin synthase; Bacillus-subtilis; 20s proteasome; Complex; Core; Acidophilum.; Cell & developmental biology.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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