2005
Correction of X‐ray intensities from an HslV–HslU co‐crystal containing lattice‐translocation defects
Wang J, Rho SH, Park HH, Eom SH. Correction of X‐ray intensities from an HslV–HslU co‐crystal containing lattice‐translocation defects. Acta Crystallographica Section D, Structural Biology 2005, 61: 932-941. PMID: 15983416, DOI: 10.1107/s0907444905009546.Peer-Reviewed Original ResearchRole 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
Unraveling the means to the end in ATP-dependent proteases
Hochstrasser M, Wang J. Unraveling the means to the end in ATP-dependent proteases. Nature Structural & Molecular Biology 2001, 8: 294-296. PMID: 11276243, DOI: 10.1038/86153.Peer-Reviewed Original Research
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
1998
Crystal Structure Determination ofEscherichia coliClpP Starting from an EM-Derived Mask
Wang J, Hartling J, Flanagan J. Crystal Structure Determination ofEscherichia coliClpP Starting from an EM-Derived Mask. Journal Of Structural Biology 1998, 124: 151-163. PMID: 10049803, DOI: 10.1006/jsbi.1998.4058.Peer-Reviewed Original ResearchConceptsATP-dependent proteolytic complexEscherichia coli ClpPATP-dependent proteaseProteolytic active sitesEvolutionary convergenceClpP structureHeptameric ringsProteolytic complexIntracellular proteolysisProteolytic componentBiophysical techniquesClpPSmall-angle X-rayX-ray crystallographyX-ray crystal structureStriking exampleMatrix refinementActive siteProteaseStructure determinationHslVOverall architectureProteasomeStructural levelElectron microscopy
1997
The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
Wang J, Hartling J, Flanagan J. The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis. Cell 1997, 91: 447-456. PMID: 9390554, DOI: 10.1016/s0092-8674(00)80431-6.Peer-Reviewed Original Research