2015
Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter
Lee Y, Min CK, Kim TG, Song HK, Lim Y, Kim D, Shin K, Kang M, Kang JY, Youn HS, Lee JG, An JY, Park KR, Lim JJ, Kim JH, Kim JH, Park ZY, Kim YS, Wang J, Kim DH, Eom SH. Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter. EMBO Reports 2015, 16: 1318-1333. PMID: 26341627, PMCID: PMC4662854, DOI: 10.15252/embr.201540436.Peer-Reviewed Original ResearchConceptsN-terminal domainMitochondrial calcium uniporterCalcium uniporterHuman mitochondrial calcium uniporterMitochondrial calcium uptake 1CaMKII phosphorylation siteDominant negative effectCell linesMitochondrial calcium uptakePhosphorylation sitesNovel foldDeletion mutantsMCU functionÅ resolutionTumor suppressorHeLa cell lineUniporterMutantsUptake 1Calcium uptakeS92SuppressorOncogeneRegulatorDomain
2013
Calcium-dependent conformational transition of calmodulin determined by Fourier transform infrared spectroscopy
Yu T, Wu G, Yang H, Wang J, Yu S. Calcium-dependent conformational transition of calmodulin determined by Fourier transform infrared spectroscopy. International Journal Of Biological Macromolecules 2013, 56: 57-61. PMID: 23403030, DOI: 10.1016/j.ijbiomac.2013.02.004.Peer-Reviewed Original ResearchMeSH KeywordsCalciumCalmodulinDeuterium Exchange MeasurementProtein Structure, SecondarySpectroscopy, Fourier Transform Infrared
2010
Insights into Base Selectivity from the 1.8 Å Resolution Structure of an RB69 DNA Polymerase Ternary Complex
Wang M, Xia S, Blaha G, Steitz TA, Konigsberg WH, Wang J. Insights into Base Selectivity from the 1.8 Å Resolution Structure of an RB69 DNA Polymerase Ternary Complex. Biochemistry 2010, 50: 581-590. PMID: 21158418, PMCID: PMC3036992, DOI: 10.1021/bi101192f.Peer-Reviewed Original Research
2005
A Twisted Four-Sheeted Model for an Amyloid Fibril
Wang J, Gülich S, Bradford C, Ramirez-Alvarado M, Regan L. A Twisted Four-Sheeted Model for an Amyloid Fibril. Structure 2005, 13: 1279-1288. PMID: 16154085, DOI: 10.1016/j.str.2005.06.010.Peer-Reviewed Original ResearchMeSH KeywordsAmyloidBacterial ProteinsHumansModels, MolecularProtein Structure, SecondaryX-Ray Diffraction
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 structureDomainMembers
2003
Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis
Yoon J, Oh B, Kim K, Park JE, Wang J, Kim HS, Kim Y. Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis. Biochemical And Biophysical Research Communications 2003, 310: 651-659. PMID: 14521961, DOI: 10.1016/j.bbrc.2003.09.056.Peer-Reviewed Original ResearchMeSH KeywordsAmidohydrolasesAmino AcidsCatalysisDimerizationHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular WeightMutagenesisProtein Structure, SecondaryConceptsCyclic amidasesD-hydantoinaseCatalytic propertiesHydrophobic interaction domainCatalytic activityEnzymatic catalysisHydrophobic interactionsCyclic ureidesReversible hydrolysisDimeric formHydrophobic patchDimeric interactionsOligomeric stateSpecific activityTetramerKinetic propertiesCatalysisLow specific activityDihydropyrimidinesPropertiesHydantoinsDimersDihydroorotaseHydrolysisInteraction
1999
Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin
Silvian L, Wang J, Steitz T. Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin. Science 1999, 285: 1074-1077. PMID: 10446055, DOI: 10.1126/science.285.5430.1074.Peer-Reviewed Original ResearchAcylationAdenosine MonophosphateAmino AcidsBinding SitesCrystallography, X-RayDNA-Directed DNA PolymeraseGlutamate-tRNA LigaseIsoleucineIsoleucine-tRNA LigaseModels, MolecularMupirocinNucleic Acid ConformationOligopeptidesProtein ConformationProtein Structure, SecondaryRNA, Transfer, GlnRNA, Transfer, IleStaphylococcus aureusSubstrate Specificity
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
Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69
Wang J, Sattar A, Wang C, Karam J, Konigsberg W, Steitz T. Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69. Cell 1997, 89: 1087-1099. PMID: 9215631, DOI: 10.1016/s0092-8674(00)80296-2.Peer-Reviewed Original ResearchBacteriophagesBinding SitesConserved SequenceCrystallographyDNA Polymerase IDNA Polymerase IIDNA, Single-StrandedEscherichia coliExonucleasesGene Expression Regulation, ViralHIVProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryReplication OriginRNA-Directed DNA PolymeraseSequence Homology, Amino Acid