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
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
2014
Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix
Brown JA, Bulkley D, Wang J, Valenstein ML, Yario TA, Steitz TA, Steitz JA. Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nature Structural & Molecular Biology 2014, 21: 633-640. PMID: 24952594, PMCID: PMC4096706, DOI: 10.1038/nsmb.2844.Peer-Reviewed Original Research
2012
The Hexameric Helicase DnaB Adopts a Nonplanar Conformation during Translocation
Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA. The Hexameric Helicase DnaB Adopts a Nonplanar Conformation during Translocation. Cell 2012, 151: 267-277. PMID: 23022319, PMCID: PMC3597440, DOI: 10.1016/j.cell.2012.09.014.Peer-Reviewed Original ResearchConceptsTranslocation mechanismParental duplex DNAReplicative DNA helicaseNucleotides of ssDNAC-terminal domainDNA helicaseDnaB hexamerHelicase DnaBNTP hydrolysisNascent DNAStructural insightsQuaternary structureDNA templateDuplex DNADNA polymeraseDnaBTranslocationSequential hydrolysisSubunitsUnwindingNucleotidesDNASsDNAHelicasesHelicase
2011
Structural Insights into Complete Metal Ion Coordination from Ternary Complexes of B Family RB69 DNA Polymerase
Xia S, Wang M, Blaha G, Konigsberg WH, Wang J. Structural Insights into Complete Metal Ion Coordination from Ternary Complexes of B Family RB69 DNA Polymerase. Biochemistry 2011, 50: 9114-9124. PMID: 21923197, PMCID: PMC3760225, DOI: 10.1021/bi201260h.Peer-Reviewed Original ResearchConceptsMetal ionsBond formationHydroxyl groupsCoordination bond lengthsMetal ion coordinationΑ-phosphateB-siteTernary complexMetal ion ACoordination complexesIon coordinationBond lengthsCoordination octahedraIon APhosphorus atomIonic radiusSimultaneous coordinationPhosphodiester bond formationIonsNucleotidyl transferStructural insightsComplexesPyrophosphate product
2005
A specific subdomain in φ29 DNA polymerase confers both processivity and strand-displacement capacity
Rodríguez I, Lázaro JM, Blanco L, Kamtekar S, Berman AJ, Wang J, Steitz TA, Salas M, de Vega M. A specific subdomain in φ29 DNA polymerase confers both processivity and strand-displacement capacity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 6407-6412. PMID: 15845765, PMCID: PMC1088371, DOI: 10.1073/pnas.0500597102.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacteriophage T4DNADNA PrimersDNA ReplicationDNA-Directed DNA PolymeraseElectrophoretic Mobility Shift AssayExodeoxyribonucleasesModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein ConformationProtein Structure, TertiarySequence AlignmentTemplates, GeneticConceptsDNA polymerasePhi29 DNA polymeraseProtein-primed DNA polymerasesStrand-displacement capacityMutant DNA polymerasesΦ29 DNA polymeraseRecent crystallographic studiesDNA binding capacityAsp-398Deletion mutantsStructural insightsSpecific insertionProcessivityPolymeraseStrand displacementFunctional roleAmino acidsPalm subdomainSpecific subdomainsBiochemical analysisDNA synthesisCritical roleRegion 2Crystallographic studiesIntrinsic capacity