2018
Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPases
Chase A, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPases. The FASEB Journal 2018, 32: 114.1-114.1. DOI: 10.1096/fasebj.2018.32.1_supplement.114.1.Peer-Reviewed Original ResearchOligomeric stateNuclear envelope defectsRobust ATPase activityExperimental Biology 2018 MeetingPresence of ATPEnvelope defectsCofactor assemblyHomotypic oligomersCellular cofactorsATP hydrolysisDynamic assemblyFunctional assemblyMolecular etiologyATPase activationLAP1Novel modeATPase activityCofactorFASEB JournalATPasesCofactor systemATPaseAssemblyDYT1 dystoniaKey role
2005
Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*
Park E, Rho YM, Koh OJ, Ahn SW, Seong IS, Song JJ, Bang O, Seol JH, Wang J, Eom SH, Chung CH. Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*. Journal Of Biological Chemistry 2005, 280: 22892-22898. PMID: 15849200, DOI: 10.1074/jbc.m500035200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCaseinsChromatographyCross-Linking ReagentsDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEndopeptidase ClpEscherichia coliEscherichia coli ProteinsGlycineHydrolysisModels, BiologicalModels, MolecularMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedMutationPeptidesProtein BindingProtein DenaturationProtein FoldingProtein TransportSequence Homology, Amino AcidTemperatureConceptsHslU ATPasePore motifHslVU complexHslV peptidaseCentral poreATP-dependent proteaseProtein unfoldingProteolytic active sitesHslU hexamerProteolytic chamberHslV dodecamerUnfolded proteinsHslV.HslUGly residueTranslocation processAmino acidsDegradation of caseinMotifProteinATP cleavageSame structural featuresATPase activityTranslocationATPase
2001
A Corrected Quaternary Arrangement of the Peptidase HslV and ATPase HslU in a Cocrystal Structure
Wang J. A Corrected Quaternary Arrangement of the Peptidase HslV and ATPase HslU in a Cocrystal Structure. Journal Of Structural Biology 2001, 134: 15-24. PMID: 11469873, DOI: 10.1006/jsbi.2001.4347.Peer-Reviewed Original ResearchConceptsQuaternary arrangementATP-dependent HslVU proteaseHslV peptidaseTranslocation poreHslU ATPaseHslVU proteaseHexameric ringHslVCocrystal structureHslUSmall-angle X-ray scattering (SAXS) studiesCrystal structurePeptidaseATPaseCrystallographic analysisElectron microscopic studySpace group assignmentX-ray scattering studyBindsHexamerProtease