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Updated: Aug 3, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy
I Gutsche1, O Mihalache, R Hegerl
1Max-Planck-Institute for Biochemistry, Am Klopferspitz 18a, D-82152, Martinsried, Germany. gutsche@biochem.mpg.de
Abstract:
Chaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. Conformational rearrangements upon ATPase cycling of the group I chaperonins, typified by the Escherichia coli GroEL/GroES system, have been thoroughly investigated by cryo-electron microscopy and X-ray crystallography. For archaeal group II chaperonins, however, these methods have so far failed to provide a correlation between the structural and the functional states. Here, we show that the conformation of the native alphabeta-thermosome of Thermoplasma acidophilum in vitrified ice is strictly regulated by adenine nucleotides.
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