2007
Crystal structure of Bacillus subtilis CodW, a noncanonical HslV‐like peptidase with an impaired catalytic apparatus
Rho S, Park HH, Kang GB, Im YJ, Kang MS, Lim BK, Seong IS, Seol J, Chung CH, Wang J, Eom SH. Crystal structure of Bacillus subtilis CodW, a noncanonical HslV‐like peptidase with an impaired catalytic apparatus. Proteins Structure Function And Bioinformatics 2007, 71: 1020-1026. PMID: 17979190, DOI: 10.1002/prot.21758.Peer-Reviewed Original Research
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 Research
2003
A second response in correcting the HslV–HslU quaternary structure
Wang J. A second response in correcting the HslV–HslU quaternary structure. Journal Of Structural Biology 2003, 141: 7-8. PMID: 12576015, DOI: 10.1016/s1047-8477(02)00629-9.Peer-Reviewed Original Research
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 studyBindsHexamerProteaseUnraveling 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 ResearchMeSH KeywordsAdenosine TriphosphatasesAdenosine TriphosphateCyanobacteriaEndopeptidase ClpEscherichia coliPlantsProtein ConformationSerine EndopeptidasesConceptsClp 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