2023
Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport
Ton W, Wang Y, Chai P, Beauchamp-Perez C, Flint N, Lammers L, Xiong H, Zhang K, Markus S. Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport. Nature Structural & Molecular Biology 2023, 30: 1365-1379. PMID: 37322240, PMCID: PMC10590275, DOI: 10.1038/s41594-023-01010-x.Peer-Reviewed Original ResearchConceptsCryo-EM structureCargo transportProtein Lis1Human dyneinDynein mutantsCytoplasmic dyneinStructural insightsDynein activityIntracellular localizationCritical regulatorDynein activationLIS1Conformational changesDyneinMotor domainMutantsBindingHigh affinityAffinityYeastMicrotubulesRegulatorRegulationTransportActivation
2022
Structures of the CcmABCD heme release complex at multiple states
Li J, Zheng W, Gu M, Han L, Luo Y, Yu K, Sun M, Zong Y, Ma X, Liu B, Lowder EP, Mendez DL, Kranz RG, Zhang K, Zhu J. Structures of the CcmABCD heme release complex at multiple states. Nature Communications 2022, 13: 6422. PMID: 36307425, PMCID: PMC9616876, DOI: 10.1038/s41467-022-34136-5.Peer-Reviewed Original ResearchConceptsHigh-resolution cryo-EM structuresResolution cryo-EM structureABC transporter complexAttachment of hemeCryo-EM structureLarge membrane complexesHeme-binding siteATP-binding siteATP-dependent releaseTransfer of hemeC-type cytochromesHeme chaperoneHeme traffickingCytochrome c proteinMembrane proteinsHeme transferTransporter complexMembrane complexATP hydrolysisStructural basisC proteinAMP-PNPFunctional studiesHeme releaseUnbound formCryo-EM structure of an active central apparatus
Han L, Rao Q, Yang R, Wang Y, Chai P, Xiong Y, Zhang K. Cryo-EM structure of an active central apparatus. Nature Structural & Molecular Biology 2022, 29: 472-482. PMID: 35578022, PMCID: PMC9113940, DOI: 10.1038/s41594-022-00769-9.Peer-Reviewed Original ResearchConceptsCentral apparatusDiverse cellular activitiesKinesin-like proteinCryo-EM structureArmadillo repeat proteinsCryo-electron microscopyHigh-resolution structuresEukaryotic speciesProtein subunitsMotile ciliaBridge proteinsPair of microtubulesRegulatory roleCellular activitiesProteinDynamic conformational behaviorCiliary motilityCiliaCiliary beatingStructural frameworkConformational behaviorSubunitsMicrotubulesRegulatorSpecies
2021
Cryo-EM structures of Escherichia coli cytochrome bo3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site
Li J, Han L, Vallese F, Ding Z, Choi SK, Hong S, Luo Y, Liu B, Chan CK, Tajkhorshid E, Zhu J, Clarke O, Zhang K, Gennis R. Cryo-EM structures of Escherichia coli cytochrome bo3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2106750118. PMID: 34417297, PMCID: PMC8403832, DOI: 10.1073/pnas.2106750118.Peer-Reviewed Original ResearchConceptsHydrogen bondsMembrane scaffold protein (MSP) nanodiscsSide chainsMetal redox centerCryo-EM structureInternal water moleculesEscherichia coli cytochrome bo3Facilitate proton transferImidazole side chainIsoprene side chainAccess of waterCryogenic electron microscopyRedox centersWater moleculesProton transferSubunit IAqueous phaseConformation 1Respiratory cytochromesRelated cytochromesHydrophobic grooveUbiquinol oxidaseQuinol oxidaseCytochrome bo3Computational studyCryo‐EM Structures of Outer‐arm Dynein Array Bound to Microtubule Doublet Reveal a Mechanism for Motor Coordination
Rao Q, Wang Y, Chai P, Kuo Y, Han L, Yang R, Yang Y, Howard J, Zhang K. Cryo‐EM Structures of Outer‐arm Dynein Array Bound to Microtubule Doublet Reveal a Mechanism for Motor Coordination. The FASEB Journal 2021, 35 DOI: 10.1096/fasebj.2021.35.s1.03099.Peer-Reviewed Original ResearchOuter arm dyneinMicrotubule-bound stateInner arm dyneinsCentral pair complexMicrotubule-binding domainMicrotubule doubletsIntermediate chainATP hydrolysisFundamental cellular processesHeavy chainCryo-EM structureCryo-EM analysisCryo-electron tomographyKey motor proteinCryo-electron microscopyLight chainCellular processesEukaryotic ciliaT. thermophilaEmbryonic developmentAdjacent microtubule doubletsCellular motilityMotor proteinsAxonemal dyneinsMotile cilia
2019
Structural basis of antagonism of human APOBEC3F by HIV-1 Vif
Hu Y, Desimmie BA, Nguyen HC, Ziegler SJ, Cheng TC, Chen J, Wang J, Wang H, Zhang K, Pathak VK, Xiong Y. Structural basis of antagonism of human APOBEC3F by HIV-1 Vif. Nature Structural & Molecular Biology 2019, 26: 1176-1183. PMID: 31792451, PMCID: PMC6899190, DOI: 10.1038/s41594-019-0343-6.Peer-Reviewed Original ResearchConceptsHIV-1 VifProtein degradation machineryCryo-EM structureHuman immunodeficiency virus type 1 (HIV-1) replicationCore-binding factor betaUbiquitin-proteasome pathwayRole of CbfβHIV-1 virion infectivity factorType 1 replicationVif-A3 interactionsViral immune evasionDegradation machineryAntiviral APOBEC3Terminal domainVirion infectivity factorStructural basisMolecular mechanismsViral restrictionA3 proteinsMolecular determinantsImmune evasionInfectivity factorFactor betaCellular studiesAntiviral therapeutics
2014
Cryo-EM structures of two bovine adenovirus type 3 intermediates
Cheng L, Huang X, Li X, Xiong W, Sun W, Yang C, Zhang K, Wang Y, Liu H, Huang X, Ji G, Sun F, Zheng C, Zhu P. Cryo-EM structures of two bovine adenovirus type 3 intermediates. Virology 2014, 450: 174-181. PMID: 24503080, DOI: 10.1016/j.virol.2013.12.012.Peer-Reviewed Original ResearchConceptsCryo-electron tomography analysisDNA encapsidation processCryo-EM structureCryo-electron microscopyVertebrate speciesFirst structural comparisonProtein VIDNA encapsidationEncapsidation processStructural comparisonProtein IXUnique conformationBackbone levelIntermediate structuresHuman ADMass spectrometryLater stagesEncapsidationSpeciesSimilar structureBAd3HostIntermediatesAssemblyCleavage
2012
Cryo-EM structure of a transcribing cypovirus
Yang C, Ji G, Liu H, Zhang K, Liu G, Sun F, Zhu P, Cheng L. Cryo-EM structure of a transcribing cypovirus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 6118-6123. PMID: 22492979, PMCID: PMC3341035, DOI: 10.1073/pnas.1200206109.Peer-Reviewed Original ResearchConceptsNascent mRNATurret proteinFamily ReoviridaeCapsid shellConformational changesCapsid proteinMRNA transcriptionCryo-EM structureMajor capsid proteinGood model systemGuanylyltransferase domainTranscription cycleViral capsid proteinsIcosahedral viral capsidsCypovirusGenomic RNACryoelectron microscopyGMP moietyRNA virusesProteinViral capsidTranscriptionMRNAReoviridaeModel system
2011
Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping
Cheng L, Sun J, Zhang K, Mou Z, Huang X, Ji G, Sun F, Zhang J, Zhu P. Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 1373-1378. PMID: 21220303, PMCID: PMC3029759, DOI: 10.1073/pnas.1014995108.Peer-Reviewed Original ResearchConceptsCytoplasmic polyhedrosis virusDeduced amino acid sequenceCryo-EM structureRNA segment 7Amino acid sequenceMechanisms of mRNANascent mRNAEnzymatic domainsAcid sequenceCryoelectron microscopyFamily ReoviridaeProtein VP5Capsid shellPolyhedrosis virusFull atomic modelsAtomic modelStructural organizationGuanylyltransferaseMRNASegment 7ProteinCypovirus