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 ResearchMeSH KeywordsAdenosine TriphosphateChaperonin 60Cryoelectron MicroscopyEscherichia coliModels, MolecularProtein BindingProtein FoldingConceptsCryo-electron microscopySalt-bridge contactsGroEL ringGroEL-GroESChaperonin GroELSalt bridge interactionsCryo-EMMolecular machinesADP complexGroELATPRing complexBridge interactionEffect of ATPCooperativityOpposite ringIntermediate domainGroESGeneral insightsComplexesPolypeptideDomainBridge contactsStructural modelAffinityFolding of malate dehydrogenase inside the GroEL–GroES cavity
Chen J, Walter S, Horwich A, Smith D. Folding of malate dehydrogenase inside the GroEL–GroES cavity. Nature Structural & Molecular Biology 2001, 8: 721-728. PMID: 11473265, DOI: 10.1038/90443.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesChaperonin 10Chaperonin 60Chromatography, High Pressure LiquidDeuteriumDimerizationHydrogen BondingKineticsMalate DehydrogenaseMass SpectrometryMitochondria, HeartModels, MolecularPeptide FragmentsProtein BindingProtein DenaturationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsSwineConceptsMalate dehydrogenaseNonnative substrate proteinGroEL-GroES cavitySubstrate proteinsProductive foldingChaperonin GroELApical domainGroESGroELMechanical unfoldingGlobal destabilizationSecondary structureHydrophilic chamberCentral cavityInitial proteinDeuterium exchangeFoldingProteinATPDehydrogenaseHydrophobic central cavityMass spectrometryOpen ringPolypeptideUnfoldingMechanisms of protein folding
Grantcharova V, Alm E, Baker D, Horwich A. Mechanisms of protein folding. Current Opinion In Structural Biology 2001, 11: 70-82. PMID: 11179895, DOI: 10.1016/s0959-440x(00)00176-7.Peer-Reviewed Original ResearchConceptsEscherichia coli chaperonin GroELNon-native proteinsATP-dependent formationCo-chaperonin GroESLowest free energy pathChaperonin GroELProtein foldingUnfolded proteinsLarge proteinsGroELNative stateNative structureContact orderProteinChaperoninKinetic trapsFoldingChaperonesGroESFree energy pathPolypeptideComplexes
2000
Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL
Farr G, Furtak K, Rowland M, Ranson N, Saibil H, Kirchhausen T, Horwich A. Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL. Cell 2000, 100: 561-573. PMID: 10721993, DOI: 10.1016/s0092-8674(00)80692-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBacterial ProteinsBinding SitesCattleChaperonin 10Chaperonin 60Chemical PhenomenaChemistry, PhysicalCryoelectron MicroscopyCystineEscherichia coliEthylmaleimideImage Processing, Computer-AssistedMacromolecular SubstancesMalate DehydrogenaseModels, MolecularPeptidesProtein BindingProtein ConformationProtein FoldingProtein Structure, TertiaryRibulose-Bisphosphate CarboxylaseStructure-Activity RelationshipThiosulfate SulfurtransferaseConceptsNonnative substrate proteinApical domainSubstrate proteinsChaperonin GroELWild-type domainCross-linking experimentsCochaperonin GroESNonnative proteinsProductive foldingGroEL ringSingle polypeptideHydrophobic residuesMalate dehydrogenaseBinary complex formationRubiscoProteinInside aspectMultivalent bindingGroELCentral cavityComplex formationBindingDomainGroESOpen ring
1998
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
Sigler P, Xu Z, Rye H, Burston S, Fenton W, Horwich A. STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. Annual Review Of Biochemistry 1998, 67: 581-608. PMID: 9759498, DOI: 10.1146/annurev.biochem.67.1.581.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateChaperonin 10Chaperonin 60Models, MolecularPeptidesProtein BindingProtein ConformationProtein FoldingConceptsProtein foldingNative stateMechanism of chaperoninsCis ternary complexAsymmetric conformational changesFinal native stateNonnative polypeptidesCochaperonin GroESGroEL ringTrans ringATP hydrolysisGenetic informationChaperonin moleculesConformational changesFolding processFoldingTernary complexPolypeptideGroESATPBiochemical investigationsFinal stepChaperoninGroELComplexesThe Hsp70 and Hsp60 Chaperone Machines
Bukau B, Horwich A. The Hsp70 and Hsp60 Chaperone Machines. Cell 1998, 92: 351-366. PMID: 9476895, DOI: 10.1016/s0092-8674(00)80928-9.Peer-Reviewed Original Research[11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL
Horwich A, Burston S, Rye H, Weissman J, Fenton W. [11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods In Enzymology 1998, 290: 141-146. PMID: 9534157, DOI: 10.1016/s0076-6879(98)90013-1.Peer-Reviewed Original ResearchConceptsBacterial chaperonin GroELGreen fluorescent proteinChaperonin GroELDouble-ring assemblyAddition of GroESDouble-ring complexesSingle-ring versionUnliganded GroELBacterial chaperoninsGroEL ringNeighboring subunitProtein foldsGroELEquatorial domainNonnative formsFluorescent proteinGroESNative stateNative formCentral channelCritical signalingSubunitsSignalingForm contactsNormal ATP
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 tiltDeadly Conformations—Protein Misfolding in Prion Disease
Horwich A, Weissman J. Deadly Conformations—Protein Misfolding in Prion Disease. Cell 1997, 89: 499-510. PMID: 9160742, DOI: 10.1016/s0092-8674(00)80232-9.Peer-Reviewed Original ResearchNative-like structure of a protein-folding intermediate bound to the chaperonin GroEL
Goldberg M, Zhang J, Sondek S, Matthews C, Fox R, Horwich A. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1080-1085. PMID: 9037009, PMCID: PMC19747, DOI: 10.1073/pnas.94.4.1080.Peer-Reviewed Original ResearchConceptsNative-like structureChaperonin GroELDihydrofolate reductaseProtein-folding intermediatesNative dihydrofolate reductaseStopped-flow fluorescence experimentsNonnative proteinsSubstrate proteinsProductive foldingPresence of ATPHuman dihydrofolate reductaseHydrogen-deuterium exchangeGroELPrimary structureProteinCentral channelHydrophobic interactionsFluorescence experimentsGroESFoldingSpeciesReductaseNMR spectroscopyDistant partsATP
1994
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
Braig K, Otwinowski Z, Hegde R, Boisvert D, Joachimiak A, Horwich A, Sigler P. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å. Nature 1994, 371: 578-586. PMID: 7935790, DOI: 10.1038/371578a0.Peer-Reviewed Original Research