Intraring allostery controls the function and assembly of a hetero‐oligomeric class II chaperonin

Class II chaperonins are essential multisubunit complexes that aid the folding of nonnative proteins in the cytosol of archaea and eukarya. They use energy derived from ATP to drive a series of structural rearrangements that enable polypeptides to fold within their central cavity. These events are r...

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Veröffentlicht in:	The FASEB journal 2018-04, Vol.32 (4), p.2223-2234
Hauptverfasser:	Shoemark, Deborah K., Sessions, Richard B., Brancaccio, Andrea, Bigotti, Maria Giulia
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Allosteric Regulation Allosteric Site Archaeal Proteins - chemistry Archaeal Proteins - metabolism Group II Chaperonins - chemistry Group II Chaperonins - metabolism molecular chaperones molecular dynamics Molecular Dynamics Simulation Protein Binding protein folding Protein Multimerization Thermoplasma - chemistry
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