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ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo‐electron microscopy
Author(s) -
Gutsche Irina,
Mihalache Oana,
Hegerl Reiner,
Typke Dieter,
Baumeister Wolfgang
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01811-1
Subject(s) - chaperonin , groel , thermoplasma acidophilum , atp hydrolysis , groes , atpase , crystallography , cryo electron microscopy , protein folding , chemistry , biochemistry , chaperone (clinical) , biophysics , biology , escherichia coli , enzyme , gene , medicine , pathology
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 αβ‐thermosome of Thermoplasma acidophilum in vitrified ice is strictly regulated by adenine nucleotides.