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

ID: 318299.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Crystal structure of the 20s proteasome from the archaeon t-acidophilum at 3.4 angstrom resolution
Authors:Löwe, J.; Stock, D.; Jap, B.; Zwickl, P.; Baumeister, W.; Huber, R.
Date of Publication (YYYY-MM-DD):1995-04-28
Title of Journal:Science
Issue / Number:5210
Start Page:533
End Page:539
Audience:Not Specified
Abstract / Description:The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha(7) beta(7) beta(7) alpha(7) subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism. [References: 68]
Free Keywords:Multicatalytic proteinase complexes; Atp-dependent proteases; Thermoplasma-acidophilum; Electron-microscopy; Escherichia-coli; Mechanism; Gene; Refinement; Peptidase; Features.; Multidisciplinary. Multidisciplinary. Multidisciplinary.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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