ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy.
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.
Gutsche
I
I
Max-Planck-Institute for Biochemistry, Am Klopferspitz 18a, D-82152, Martinsried, Germany. gutsche@biochem.mpg.de
Mihalache
O
O
Hegerl
R
R
Typke
D
D
Baumeister
W
W
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D019843:Archaeal Proteins / Q000737:chemistry*; D018833:Chaperonins / Q000737:chemistry*; D020285:Cryoelectron Microscopy; D011487:Protein Conformation
D019843:Archaeal Proteins; D000251:Adenosine Triphosphatases; D018833:Chaperonins