2022
Structural Insights into Binding of Remdesivir Triphosphate within the Replication–Transcription Complex of SARS-CoV‑2
Wang J, Shi Y, Reiss K, Maschietto F, Lolis E, Konigsberg WH, Lisi GP, Batista VS. Structural Insights into Binding of Remdesivir Triphosphate within the Replication–Transcription Complex of SARS-CoV‑2. Biochemistry 2022, 61: 1966-1973. PMID: 36044776, PMCID: PMC9469760, DOI: 10.1021/acs.biochem.2c00341.Peer-Reviewed Original ResearchConceptsReplication-transcription complexStructural basisCryo-EM structureAdenosine monophosphateRemdesivir triphosphateStructural insightsDuplex productsPrimer extensionNucleotide selectivityBase pairsNucleotide incorporationIncoming substrateRibosyl moietyActive complexSARS-CoV-2 inhibitorsNew detailed informationTriphosphateComplexesMolecular dynamics simulationsAdenosine triphosphate
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
2004
Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily
Wang J. Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily. Journal Of Structural Biology 2004, 148: 259-267. PMID: 15522774, DOI: 10.1016/j.jsb.2004.07.003.Peer-Reviewed Original ResearchConceptsNucleotide-dependent conformational changesT7 DNA helicaseImportant biological functionsMechanochemical motorOligomeric ringsDNA helicaseBiological functionsF1-ATPaseConformational changesDomain motionProteinMechanistic workForce generationHslUHelicaseFoldsChemical energyATPFamilyRing structureDomainMembersVisualizing a Circadian Clock Protein Crystal Structure of KaiC and Functional Insights
Pattanayek R, Wang J, Mori T, Xu Y, Johnson CH, Egli M. Visualizing a Circadian Clock Protein Crystal Structure of KaiC and Functional Insights. Molecular Cell 2004, 15: 375-388. PMID: 15304218, DOI: 10.1016/j.molcel.2004.07.013.Peer-Reviewed Original ResearchConceptsClock protein complexesAuto-phosphorylation siteGlobal gene expressionCircadian biological clockHomohexameric complexEvolutionary relationshipsProtein complexesCircadian clockworkATP bindingFunctional insightsCircadian proteinsKaiCProtein crystal structuresCentral poreGene expressionMolecular componentsBiochemical mechanismsBiological clockCrystal structureDouble donutComplex formationProteinCircadian rhythmicityMutationsCyanobacteria
2003
Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide Complexes
Xiong Y, Li F, Wang J, Weiner AM, Steitz TA. Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide Complexes. Molecular Cell 2003, 12: 1165-1172. PMID: 14636575, DOI: 10.1016/s1097-2765(03)00440-4.Peer-Reviewed Original ResearchConceptsCCA-adding enzymeClass I CCA-adding enzymeCrystal structureClose evolutionary relationshipAddition of CCAChemical modificationAmino acid sequenceElectrostatic charge distributionNucleic acid templateEvolutionary relationshipsImmature tRNAsCharge distributionDomain architectureNucleotide complexesArcheoglobus fulgidusEnzyme classesTail domainAcid sequenceEnzyme bindsPolymerase domainTRNARelative orientationComplexesEnzymeTerminusDomain Motions in GroEL upon Binding of an Oligopeptide
Wang J, Chen L. Domain Motions in GroEL upon Binding of an Oligopeptide. Journal Of Molecular Biology 2003, 334: 489-499. PMID: 14623189, DOI: 10.1016/j.jmb.2003.09.074.Peer-Reviewed Original ResearchA 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
Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP
Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA. Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP. Cell 2002, 111: 815-824. PMID: 12526808, DOI: 10.1016/s0092-8674(02)01115-7.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCrystallography, X-RayCytidine TriphosphateDimerizationDNA Polymerase betaGeobacillus stearothermophilusModels, MolecularMolecular Sequence DataProtein FoldingProtein Structure, TertiaryRNA NucleotidyltransferasesSequence Homology, Amino AcidConceptsCCA-adding enzymeResolution crystal structureDNA polymerase betaImmature tRNAsNew proteinsBase specificityNucleic acid templateBacillus stearothermophilusPalm domainPolymerase betaIncoming ATPTRNAATPTerminusSubunitsCrystal structureActive siteAdditional structural featuresEnzymeCTPStructural featuresComplexesImportant componentTailDomain
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
1996
The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
Boisvert D, Wang J, Otwinowski Z, Norwich A, Sigler P. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nature Structural & Molecular Biology 1996, 3: 170-177. PMID: 8564544, DOI: 10.1038/nsb0296-170.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceBinding SitesChaperonin 60Crystallography, X-RayMagnesiumModels, MolecularMolecular Sequence DataProtein Conformation