2001
ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy
Ranson N, Farr G, Roseman A, Gowen B, Fenton W, Horwich A, Saibil H. ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy. Cell 2001, 107: 869-879. PMID: 11779463, DOI: 10.1016/s0092-8674(01)00617-1.Peer-Reviewed Original ResearchConceptsCryo-electron microscopySalt-bridge contactsGroEL ringGroEL-GroESChaperonin GroELSalt bridge interactionsCryo-EMMolecular machinesADP complexGroELATPRing complexBridge interactionEffect of ATPCooperativityOpposite ringIntermediate domainGroESGeneral insightsComplexesPolypeptideDomainBridge contactsStructural modelAffinityAllostery and protein substrate conformational change during GroEL/GroES-mediated protein folding
Saibil H, Horwich A, Fenton W. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Advances In Protein Chemistry 2001, 59: 45-72. PMID: 11868280, DOI: 10.1016/s0065-3233(01)59002-6.Peer-Reviewed Original ResearchConceptsProtein foldingATP-dependent protein foldingChloroplasts of eukaryotesDouble-ring complexesCo-chaperonin GroESC-terminal portionChaperonin machineProtein folding reactionChaperonin systemSubstrate polypeptidesChaperonin complexGroEL-GroESHeptameric ringsGroEL subunitStructural biologyBiophysical approachesEquatorial domainATPase mechanismConformational changesSubstrate conformational changesFolding reactionNative formGroESFoldingGroEL
1997
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 tiltGroEL‐Mediated protein folding
Fenton W, Horwich A. GroEL‐Mediated protein folding. Protein Science 1997, 6: 743-760. PMID: 9098884, PMCID: PMC2144759, DOI: 10.1002/pro.5560060401.Peer-Reviewed Original ResearchConceptsGroEL-GroESNonnative polypeptidesSubstrate proteinsATP bindingProtein foldingHomologous proteinsNonnative formsPrimary structureConformational changesGroELTernary complexPolypeptideAssociation 5FoldingProteinBindingChaperonesGroESConformationEnergy landscapeRole of hydrophobicityPathway 3RolePathwayComplex C.
1996
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
Weissman J, Rye H, Fenton W, Beechem J, Horwich A. Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction. Cell 1996, 84: 481-490. PMID: 8608602, DOI: 10.1016/s0092-8674(00)81293-3.Peer-Reviewed Original ResearchConceptsCis ternary complexProtein foldingRelease of GroESAddition of GroESFolding reactionTernary complexNonhydrolyzable ATP analogGroES releaseProtein folding reactionSubstrate proteinsPresence of ATPGroEL mutantGroEL-GroESGroEL complexNonnative substratesATP hydrolysisGroESComplete foldingSubstrate flexibilityATP analogFoldingFluorescence anisotropyActive stateATPRecent studies