2022
Cryo-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
2017
Crystal structure of E. coli apolipoprotein N-acyl transferase
Lu G, Xu Y, Zhang K, Xiong Y, Li H, Cui L, Wang X, Lou J, Zhai Y, Sun F, Zhang XC. Crystal structure of E. coli apolipoprotein N-acyl transferase. Nature Communications 2017, 8: 15948. PMID: 28885614, PMCID: PMC5500890, DOI: 10.1038/ncomms15948.Peer-Reviewed Original ResearchConceptsApolipoprotein N-acyl transferaseN-acyl transferaseTM domainN-terminal cysteine residueThree-step pathwayGram-negative bacteriaLid loopTransmembrane domainPeriplasmic sideTM helicesCysteine residuesLipid modificationLipid donorCatalytic cavityAcceptor substrateLipid bilayersLipid leafletCatalytic centerAcyl chainsCrystal structurePathwayTransferaseLateral openingDomainProteinCryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated
Zhang K, Foster HE, Rondelet A, Lacey SE, Bahi-Buisson N, Bird AW, Carter AP. Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated. Cell 2017, 169: 1303-1314.e18. PMID: 28602352, PMCID: PMC5473941, DOI: 10.1016/j.cell.2017.05.025.Peer-Reviewed Original ResearchConceptsStructure-based mutagenesisCryoelectron microscopy structureCargo adaptor proteinsMicroscopy structureAdaptor proteinCytoplasmic dyneinMicrotubule affinityCryo-EMDynein 1DynactinOpen formDynein tailInhibited stateProcessive movementMotor domainMicrotubulesMotor dimerizationTransport machinesHigh affinityMutagenesisDyneinTailAffinityProteinDimerization
2013
Structural Insights into the Intrinsic Self-Assembly of Par-3 N-Terminal Domain
Zhang Y, Wang W, Chen J, Zhang K, Gao F, Gao B, Zhang S, Dong M, Besenbacher F, Gong W, Zhang M, Sun F, Feng W. Structural Insights into the Intrinsic Self-Assembly of Par-3 N-Terminal Domain. Structure 2013, 21: 997-1006. PMID: 23643951, DOI: 10.1016/j.str.2013.04.004.Peer-Reviewed Original ResearchConceptsN-terminal domainPAR-3PAR-3/PARCell polarity establishmentPolarity establishmentEpithelial polarizationScaffold proteinProtein domainsLongitudinal packingStructural basisStructural insightsCryoelectron microscopyCentral organizerFilament-like structuresC complexFilament structureSelf-association capacitySelf-associationUnderlying mechanismDomainElectrostatic interactionsInteraction modesProteinCrystal structure
2012
Mechanistic Insights into Regulated Cargo Binding by ACAP1 Protein*
Bai M, Pang X, Lou J, Zhou Q, Zhang K, Ma J, Li J, Sun F, Hsu VW. Mechanistic Insights into Regulated Cargo Binding by ACAP1 Protein*. Journal Of Biological Chemistry 2012, 287: 28675-28685. PMID: 22645133, PMCID: PMC3436524, DOI: 10.1074/jbc.m112.378810.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsCargo bindingIntegrin recyclingRegulated transportArf6 GTPase-activating ProteinsADP-ribosylation factor (ARF) familyVesicular transport pathwaysMechanistic insightsEndocytic recyclingCoat complexSmall GTPasesCytoplasmic domainCoat componentsFurther mechanistic insightsProtein cargoFactor familyACAP1Functional studiesIntegrin β1Critical sequencesPhosphorylationBindingTransport pathwaysProteinCargoCryo-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
2010
Crystal Structure of Group II Chaperonin in the Open State
Huo Y, Hu Z, Zhang K, Wang L, Zhai Y, Zhou Q, Lander G, Zhu J, He Y, Pang X, Xu W, Bartlam M, Dong Z, Sun F. Crystal Structure of Group II Chaperonin in the Open State. Structure 2010, 18: 1270-1279. PMID: 20947016, PMCID: PMC3048791, DOI: 10.1016/j.str.2010.07.009.Peer-Reviewed Original ResearchConceptsGroup II chaperoninLid domainConformational changesOpen stateATP-dependent mannerHigh-resolution structuresDetailed conformational changesFunctional cycleThermosomeHydrophobic patchStructural comparisonProtease K digestionChaperoninClosed stateK digestionCrystal structureStructural fittingOpen formComplete crystal structureClosed structureSpeciesDomainProteinATPElectron microscopy