2017
Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima
An JY, Sharif H, Kang GB, Park KJ, Lee JG, Lee S, Jin MS, Song JJ, Wang J, Eom SH. Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima. Biochemical And Biophysical Research Communications 2017, 495: 1201-1207. PMID: 29180014, DOI: 10.1016/j.bbrc.2017.11.158.Peer-Reviewed Original ResearchConceptsPeriplasmic domainMisfolded membrane proteinsATP-dependent proteaseMembrane protein complexesResolution crystal structureHydrophobic membrane environmentMembrane homeostasisProtein complexesMembrane proteinsTransmembrane proteinMembrane environmentThermotoga maritimaStructural insightsFtsHProtease domainToxic proteinsProteinOligomerizationHigh energetic barrierDomainTranslocatesEnergetic barrierMaritimaHomeostasisCrystal structure
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
2014
The mechanism of Torsin ATPase activation
Brown RS, Zhao C, Chase AR, Wang J, Schlieker C. The mechanism of Torsin ATPase activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: e4822-e4831. PMID: 25352667, PMCID: PMC4234599, DOI: 10.1073/pnas.1415271111.Peer-Reviewed Original Research
2010
Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand
Cortajarena AL, Wang J, Regan L. Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand. The FEBS Journal 2010, 277: 1058-1066. PMID: 20089039, DOI: 10.1111/j.1742-4658.2009.07549.x.Peer-Reviewed Original ResearchConceptsTPR domainC-terminusKey protein-protein interactionsTetratricopeptide repeat modulesChaperone heat shock proteinProtein-protein interactionsHeat shock responseHeat shock proteinsTPR proteinsChaperone functionTPR unitsProtein domainsNew packing arrangementRepeat modulesMolecular basisPeptide ligandsShock proteinsShock responseHsp90Terminal residuesX-ray crystal structureProteinCrystal structureDomainTetratricopeptide
2009
Combining electron crystallography and X-ray crystallography to study the MlotiK1 cyclic nucleotide-regulated potassium channel
Clayton GM, Aller SG, Wang J, Unger V, Morais-Cabral JH. Combining electron crystallography and X-ray crystallography to study the MlotiK1 cyclic nucleotide-regulated potassium channel. Journal Of Structural Biology 2009, 167: 220-226. PMID: 19545635, PMCID: PMC2922748, DOI: 10.1016/j.jsb.2009.06.012.Peer-Reviewed Original ResearchConceptsS1-S4 domainMembrane protein structure determinationTetrameric cation channelsX-ray crystallographyProtein structure determinationPotassium channelsElectron crystallographyMlotiK1Cation channelsX-ray structureNew insightsProjection mapStructure determinationCrystallographyCombined applicationDomainUseful strategyQuality crystals
2006
The ϕ29 DNA polymerase:protein‐primer structure suggests a model for the initiation to elongation transition
Kamtekar S, Berman AJ, Wang J, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TA. The ϕ29 DNA polymerase:protein‐primer structure suggests a model for the initiation to elongation transition. The EMBO Journal 2006, 25: 1335-1343. PMID: 16511564, PMCID: PMC1422159, DOI: 10.1038/sj.emboj.7601027.Peer-Reviewed Original ResearchConceptsTerminal proteinDNA polymeraseDNA synthesisPrime replicationLinear chromosomesElongation transitionϕ29 DNA polymeraseBacteriophage genomesProtein movesBacteriophage phi29Resolution structureDuplex productsElongation phaseBinding cleftThird domainPolymeraseTemplate DNADuplex DNAPrimer strandSerine hydroxylProteinAbsolute requirementDNAActive siteDomain
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
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
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 Research