2024
Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni
Chen Y, Tachiyama S, Li Y, Feng X, Zhao H, Wu Y, Guo Y, Lara-Tejero M, Hua C, Liu J, Gao B. Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 122: e2412594121. PMID: 39793078, PMCID: PMC11725899, DOI: 10.1073/pnas.2412594121.Peer-Reviewed Original ResearchConceptsFlagellar motorPilZ domain-containing proteinsBound cyclic di-GMPCyclic di-GMPC-di-GMPDomain-containing proteinsStator unitsDi-GMPFamily proteinsSuperfamily proteinsBacterial flagellaRing assemblyCellular pathwaysCampylobacter jejuniCryoelectron tomographyCampylobacter jejuni</i>.Subtomogram averagingPilZProteinFlagellaPhylumAncestorMotilityJejuniStructural componentsPilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa
Guo S, Chang Y, Brun Y, Howell P, Burrows L, Liu J. PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa. Nature Communications 2024, 15: 9382. PMID: 39477930, PMCID: PMC11525922, DOI: 10.1038/s41467-024-53638-y.Peer-Reviewed Original ResearchConceptsPilus extensionCell envelopeType IV piliPathogen Pseudomonas aeruginosaBacterial cell envelopeP. aeruginosa cellsCryo-electron tomographyPilus dynamicsPilin subunitSecretin channelSurface motilityPriming complexOuter membraneBiofilm formationT4PPilY1P. aeruginosaPseudomonas aeruginosaCentral poreMolecular mechanismsSubtomogram averagingPotential therapeutic targetDynamic assemblyTherapeutic targetMolecular frameworkStructure and inhibition of SARS-CoV-2 spike refolding in membranes
Grunst M, Qin Z, Dodero-Rojas E, Ding S, Prévost J, Chen Y, Hu Y, Pazgier M, Wu S, Xie X, Finzi A, Onuchic J, Whitford P, Mothes W, Li W. Structure and inhibition of SARS-CoV-2 spike refolding in membranes. Science 2024, 385: 757-765. PMID: 39146425, PMCID: PMC11449073, DOI: 10.1126/science.adn5658.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralBetacoronavirusCell MembraneCOVID-19Cryoelectron MicroscopyElectron Microscope TomographyHumansMolecular Dynamics SimulationPeptidyl-Dipeptidase AProtein DomainsProtein MultimerizationProtein RefoldingSARS-CoV-2Spike Glycoprotein, CoronavirusVirus Internalization
2023
Cryo-electron tomography of intact cardiac muscle reveals myosin binding protein-C linking myosin and actin filaments
Huang X, Torre I, Chiappi M, Yin Z, Vydyanath A, Cao S, Raschdorf O, Beeby M, Quigley B, de Tombe P, Liu J, Morris E, Luther P. Cryo-electron tomography of intact cardiac muscle reveals myosin binding protein-C linking myosin and actin filaments. Journal Of Muscle Research And Cell Motility 2023, 44: 165-178. PMID: 37115473, PMCID: PMC10542292, DOI: 10.1007/s10974-023-09647-3.Peer-Reviewed Original ResearchConceptsMyBP-CMyosin-binding protein CCryo-electron tomographyStripes 4Binding protein CRod-shaped proteinN-terminal domainC-terminal regionCardiac MyBP-CActin filamentsAccessory proteinsCentral domainMyosin headsSubtomogram averagingActinMyosinTokuyasu cryosectionsProtein CCardiac muscleFilamentsProteinStripesC-zoneDependent fashionA-band
2021
Structural insights into the cause of human RSPH4A primary ciliary dyskinesia
Zhao Y, Pinskey J, Lin J, Yin W, Sears P, Daniels L, Zariwala M, Knowles M, Ostrowski L, Nicastro D. Structural insights into the cause of human RSPH4A primary ciliary dyskinesia. Molecular Biology Of The Cell 2021, 32: 1202-1209. PMID: 33852348, PMCID: PMC8351563, DOI: 10.1091/mbc.e20-12-0806.Peer-Reviewed Original ResearchConceptsStructural basisCryo-electron tomographyRadial spokesCentral pair complexUnderlying structural basisAxonemal repeatEukaryotic organellesArch domainThree-dimensional structureSubtomogram averagingOrgan positioningCell motilityStructural insightsPrimary ciliary dyskinesiaCiliaHuman ciliaHuman respiratory ciliaRS1Primary defectStructure determinationCiliary dyskinesiaHuman healthOrganellesFlagellaRepeats
2020
Analysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding
Park D, Chetrit D, Hu B, Roy CR, Liu J. Analysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding. MBio 2020, 11: 10.1128/mbio.03328-19. PMID: 32071271, PMCID: PMC7029142, DOI: 10.1128/mbio.03328-19.Peer-Reviewed Original ResearchConceptsType IV secretion systemSecretion systemCryoelectron tomographyInner membraneDot/Icm apparatusConformational changesDot/IcmEukaryotic host cellsBacterial inner membraneWild-type cellsHost cell membraneWhole-cell contextMultiprotein nanomachineSubtomogram analysisSophisticated nanomachinesCytoplasmic substratesProtein effectorsCell polesDNA substratesSubtomogram averagingATPase complexDNA transferHost infectionStructural basisHost cells
2019
In Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography
Zhu S, Schniederberend M, Zhitnitsky D, Jain R, Galán JE, Kazmierczak BI, Liu J. In Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography. Journal Of Bacteriology 2019, 201: 10.1128/jb.00117-19. PMID: 31010901, PMCID: PMC6560136, DOI: 10.1128/jb.00117-19.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyBacterial flagellaFlagellar assemblyPolar flagellumPeritrichous flagellaSerovar TyphimuriumSpecies-specific featuresBacterial pathogensOuter membrane complexSelf-assembling nanomachineFlagellar systemFlagellar structureFlagellar numberSubtomogram averagingMembrane complexLateral flagellaStructural basisDistinct flagellaMolecular machinesFlagellaSitu structureModel systemPseudomonasTyphimuriumRange of variation
2015
Dimeric Organization of Blood Coagulation Factor VIII bound to Lipid Nanotubes
Dalm D, Galaz-Montoya J, Miller J, Grushin K, Villalobos A, Koyfman A, Schmid M, Stoilova-McPhie S. Dimeric Organization of Blood Coagulation Factor VIII bound to Lipid Nanotubes. Scientific Reports 2015, 5: 11212. PMID: 26082135, PMCID: PMC4469981, DOI: 10.1038/srep11212.Peer-Reviewed Original ResearchConceptsMembrane-bound factor VIIIMembrane-binding domainCryo-electron microscopyMembrane-bound structuresSerine protease factor IXaDeficiency of FVIIIDimeric organizationSubtomogram averagingComplex assemblyHelical reconstructionLipid nanotubesCritical functionsFactor IXaBlood coagulationBlood coagulation factor VIIIStructural informationCrystal structureCritical stepPlatelet membranesPlatelet surfaceSevere bleeding disorderCoagulation factor VIIIIntermediate resolutionBleeding disorderMembrane
2012
Conserved structural motifs in the central pair complex of eukaryotic flagella
Carbajal‐González B, Heuser T, Fu X, Lin J, Smith BW, Mitchell DR, Nicastro D. Conserved structural motifs in the central pair complex of eukaryotic flagella. Cytoskeleton 2012, 70: 101-120. PMID: 23281266, PMCID: PMC3914236, DOI: 10.1002/cm.21094.Peer-Reviewed Original ResearchConceptsCentral pair complexCilia/flagellaRemarkable structural conservationGreen alga ChlamydomonasConserved Structural MotifCryo-electron tomographyOrganism-specific differencesEukaryotic cellsSea urchin StrongylocentrotusEvolutionary distanceStructural conservationAlga ChlamydomonasThree-dimensional structureSubtomogram averagingEukaryotic flagellaAxonemal dyneinsPrecise regulationInner proteinsMotility regulatorHair-like appendagesSinglet microtubulesChlamydomonasHuman diseasesDoublet microtubulesFlagellaCryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein
Heuser T, Barber CF, Lin J, Krell J, Rebesco M, Porter ME, Nicastro D. Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: e2067-e2076. PMID: 22733763, PMCID: PMC3409752, DOI: 10.1073/pnas.1120690109.Peer-Reviewed Original ResearchConceptsI1 dyneinCryoelectron tomographyGel-based proteomicsInner arm dyneinsCiliary assemblySensory organellesSubtomogram averagingDynein activityCritical regulatorDyneinPolypeptide compositionDoublet microtubulesBiochemical comparisonMotor domainCiliary motilityFlagellar beatingUnique interactionsCiliary beatingMotilityEukaryotesAssemblyChlamydomonasSubcomplexMutantsCiliopathiesThe structural heterogeneity of radial spokes in cilia and flagella is conserved
Lin J, Heuser T, Carbajal‐González B, Song K, Nicastro D. The structural heterogeneity of radial spokes in cilia and flagella is conserved. Cytoskeleton 2012, 69: 88-100. PMID: 22170736, PMCID: PMC3307805, DOI: 10.1002/cm.21000.Peer-Reviewed Original ResearchConceptsFlagellar motilityRadial spokesNexin-dynein regulatory complexRegulatory complexFlagellar structureMost organismsThree-dimensional structureSubtomogram averagingCryoelectron tomographyDynein motorsDynein activityChlamydomonas flagellaMotile ciliaFlagellaSperm flagellaUbiquitous componentOrganismsFunctional differencesEssential roleCiliaRepeat unitsUnprecedented detailBasal partRS1Motility
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