2002
The C-terminal Tails of HslU ATPase Act as a Molecular Switch for Activation of HslV Peptidase*
Seong IS, Kang MS, Choi MK, Lee JW, Koh OJ, Wang J, Eom SH, Chung CH. The C-terminal Tails of HslU ATPase Act as a Molecular Switch for Activation of HslV Peptidase*. Journal Of Biological Chemistry 2002, 277: 25976-25982. PMID: 12011053, DOI: 10.1074/jbc.m202793200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAmino Acid SubstitutionATP-Dependent ProteasesBinding SitesElectrophoresis, Polyacrylamide GelEndopeptidasesEnzyme ActivationHeat-Shock ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein ConformationSerine EndopeptidasesStructure-Activity RelationshipConceptsC-terminal tailHslV peptidaseHslVU complexC-terminusHexameric ringMolecular switchATP-dependent proteaseC-terminal 10 residuesAmino acidsProteolytic active sitesDodecamer consistingHslU hexamerHslU ATPaseTail peptideAxial poreATPase actsPolypeptide substratesSubstrate entryS proteasomeHslUCentral poreTerminusHslVPeptidaseCritical role
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
1999
New insights into the ATP‐dependent Clp protease: Escherichia coli and beyond
Porankiewicz J, Wang J, Clarke A. New insights into the ATP‐dependent Clp protease: Escherichia coli and beyond. Molecular Microbiology 1999, 32: 449-458. PMID: 10320569, DOI: 10.1046/j.1365-2958.1999.01357.x.Peer-Reviewed Original ResearchConceptsClp proteaseClpP proteinATP-dependent Clp proteaseClp/Hsp100Escherichia coliKey metabolic enzymesPrecise regulatory mechanismsChaperone subunitsPhotosynthetic organismsHigher plantsRegulatory subunitCellular processesHeptameric ringsHexameric ringThree-dimensional structureProteolytic subunitNew insightsRegulatory mechanismsProtein turnoverMetabolic enzymesFunctional importanceSubunitsProteaseRecent findingsProtein