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Schlagwörter:
Chaperonin; Thermosome; Cryo-electron microscopy; Atpase cycle; Thermoplasma acidophilum.; Group-ii chaperonin; Thermoplasma-acidophilum; Crystal-structure; Groel; Cct.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
Zusammenfassung:
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 alpha beta-thermosome of Thermoplasma acidophilum in vitrified ice is strictly regulated by adenine nucleotides. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. [References: 18]
