Long Han
Associate Research Scientist in PharmacologyCards
About
Research
Publications
2023
Author Correction: Cryo-EM structure of an active central apparatus
Han L, Rao Q, Yang R, Wang Y, Chai P, Xiong Y, Zhang K. Author Correction: Cryo-EM structure of an active central apparatus. Nature Structural & Molecular Biology 2023, 30: 564-564. PMID: 36899097, PMCID: PMC10113143, DOI: 10.1038/s41594-023-00961-5.Peer-Reviewed Original Research
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 formQuinol oxidases in the superfamily of heme-copper oxidoreductases and the cryoEM structure of the cytochrome bo3 ubiquinol oxidase from E. coli
Gennis R, Li J, Han L, Vallese F, Ding Z, Choi S, Hong S, Luo Y, Liu B, Chan C, Tajkhorshid E, Zhu J, Clarke O, Zhang K, Murali R, Hemp J. Quinol oxidases in the superfamily of heme-copper oxidoreductases and the cryoEM structure of the cytochrome bo3 ubiquinol oxidase from E. coli. Biochimica Et Biophysica Acta (BBA) - Bioenergetics 2022, 1863: 148667. DOI: 10.1016/j.bbabio.2022.148667.Peer-Reviewed Original Research
2021
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism
Rao Q, Han L, Wang Y, Chai P, Kuo YW, Yang R, Hu F, Yang Y, Howard J, Zhang K. Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism. Nature Structural & Molecular Biology 2021, 28: 799-810. PMID: 34556869, PMCID: PMC8500839, DOI: 10.1038/s41594-021-00656-9.Peer-Reviewed Original ResearchConceptsOuter arm dyneinMicrotubule doubletsDistinct microtubule-binding domainsHigh-resolution structuresAction of dyneinsMicrotubule-binding domainNative tracksATP hydrolysisDynein motorsHydrolyze ATPConformational changesNucleotide cycleMotor coordination mechanismATP turnoverDyneinHead interactionsMechanical forcesCryo-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
2020
Structures of the β‐barrel assembly machine recognizing outer membrane protein substrates
Xiao L, Han L, Li B, Zhang M, Zhou H, Luo Q, Zhang X, Huang Y. Structures of the β‐barrel assembly machine recognizing outer membrane protein substrates. The FASEB Journal 2020, 35: e21207. PMID: 33368572, DOI: 10.1096/fj.202001443rr.Peer-Reviewed Original ResearchConceptsBAM complexFirst β-strandOMP substratesΒ-strandsΒ-barrel outer membrane proteinsΒ-barrel assembly machinery (BAM) complexΒ-barrel assembly machineAssembly machinery complexBamA β-barrelChaperone-bound stateMembrane protein substratesRelated functional analysisLast β-strandFundamental biological processesOuter membrane proteinsDifferent conformational statesOMP biogenesisNutrition acquisitionGram-negative bacteriaProtein substratesMembrane proteinsΒ-barrelFunctional analysisBiological processesConformational states
2019
Conformational Dynamics, Intramolecular Domain Conformation Signaling, and Activation of Apo-FimD Revealed by Single-Molecule Fluorescence Resonance Energy Transfer Studies
Liu Y, Sun C, Han L, Yu Y, Zhou H, Shao Q, Lou J, Zhao Y, Huang Y. Conformational Dynamics, Intramolecular Domain Conformation Signaling, and Activation of Apo-FimD Revealed by Single-Molecule Fluorescence Resonance Energy Transfer Studies. Biochemistry 2019, 58: 1931-1941. PMID: 30888187, DOI: 10.1021/acs.biochem.9b00080.Peer-Reviewed Original ResearchConceptsC-terminal domainSingle-molecule fluorescence resonance energy transfer studiesN-terminal domainFluorescence resonance energy transfer studiesResonance energy transfer studiesConformational changesBacterial protein secretion systemsProtein secretion systemChaperone-subunit complexesDomain conformational changesSubstrate-bound stateOuter membrane proteinsPlug domainPilus biogenesisSubunit polymerizationSecretion pathwaySecretion systemMembrane proteinsDomain conformationConformational dynamicsMolecular eventsMolecular machinesEnergy transfer studiesConformational statesLinking studies
2016
Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins
Han L, Zheng J, Wang Y, Yang X, Liu Y, Sun C, Cao B, Zhou H, Ni D, Lou J, Zhao Y, Huang Y. Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins. Nature Structural & Molecular Biology 2016, 23: 192-196. PMID: 26900875, DOI: 10.1038/nsmb.3181.Peer-Reviewed Original Research