The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Xu Z, Horwich A, Sigler P. The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex. Nature 1997, 388: 741-750. PMID: 9285585, DOI: 10.1038/41944.Peer-Reviewed Original ResearchConceptsGroEL-GroESApical domainCis ringMulti-subunit protein assembliesCo-chaperonin GroESRings of subunitsPeptide-binding residuesChaperonin complexConsumption of ATPProtein foldingGroEL subunitProtein assembliesTrans ringAllosteric mechanismGroESEquatorial domainBloc movementDouble toroidSecond GroESEscherichia coliOutward tiltAsymmetric intermediatesCentral cavitySubunitsInward tiltDistinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
Rye H, Burston S, Fenton W, Beechem J, Xu Z, Sigler P, Horwich A. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 1997, 388: 792-798. PMID: 9285593, DOI: 10.1038/42047.Peer-Reviewed Original ResearchConceptsTrans ringProductive foldingGroES complexChaperonin GroELCis ringCo-chaperone GroESDouble-ring complexesCis ternary complexNon-hydrolysable ATPHydrolysis of ATPGroEL functionGroEL-ATPATP bindingEfficient foldingBinds ATPATP hydrolysisGroESMutant formsMalate dehydrogenaseGroELAMP-PNPDouble-ring structureFoldingTernary complexATP