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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.

Author: J Löwe Affiliation: Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried, Germany.D StockB JapP ZwicklW BaumeisterAll authors
Edition/Format: Article Article : English
Publication:Science (New York, N.Y.) 1995 Apr 28; 268(5210): 533-9
Summary:
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  Read more...
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Document Type: Article
All Authors / Contributors: J Löwe Affiliation: Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried, Germany.; D Stock; B Jap; P Zwickl; W Baumeister; R Huber
ISSN:0036-8075
Language Note: English
Unique Identifier: 117901549
Awards:

Abstract:

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.

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