The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL

Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two back-to-back seven-membered rings of GroEL plays an important role in regulating binding and release o...

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Veröffentlicht in:	Cell 1996-10, Vol.87 (2), p.241-251
Hauptverfasser:	Roseman, Alan M, Chen, Shaoxia, White, Helen, Braig, Kerstin, Saibil, Helen R
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Allosteric Regulation Bacterial Proteins - physiology Binding Sites Chaperonin 10 - physiology Chaperonin 60 - physiology Escherichia coli Macromolecular Substances Microscopy, Electron Models, Molecular Movement Protein Structure, Tertiary
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