Crystal structure of the 20s proteasome from the archaeon t-acidophilum at 3.4 
angstrom resolution

Löwe, J.; Stock, D.; Jap, B.; Zwickl, P.; Baumeister, W.; Huber, R.

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Crystal structure of the 20s proteasome from the archaeon t-acidophilum at 3.4 angstrom resolution

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Löwe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., & Huber, R. (1995). Crystal structure of the 20s proteasome from the archaeon t-acidophilum at 3.4 angstrom resolution. Science, 268(5210), 533-539.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7339-5

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. [References: 68]