2022
FliL ring enhances the function of periplasmic flagella
Guo S, Xu H, Chang Y, Motaleb MA, Liu J. FliL ring enhances the function of periplasmic flagella. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2117245119. PMID: 35254893, PMCID: PMC8931381, DOI: 10.1073/pnas.2117245119.Peer-Reviewed Original ResearchConceptsFlagellar motorBacterial motilityCryo-electron tomographyStator complexFlagellar proteinsMutant cellsPeriplasmic flagellaActive conformationSitu structureFascinating questionsSupramolecular complexesMotilityComplexesMotBOptimal functionFliLFlagellaIon fluxProteinFunctionAssemblyRemodelingCellsConformationBorrelia
2020
Molecular mechanism for rotational switching of the bacterial flagellar motor
Chang Y, Zhang K, Carroll BL, Zhao X, Charon NW, Norris SJ, Motaleb MA, Li C, Liu J. Molecular mechanism for rotational switching of the bacterial flagellar motor. Nature Structural & Molecular Biology 2020, 27: 1041-1047. PMID: 32895555, PMCID: PMC8129871, DOI: 10.1038/s41594-020-0497-2.Peer-Reviewed Original ResearchConceptsBacterial flagellar motorSwitch proteinFlagellar motorResponse regulator CheYRotational switchingProton motive forceSwitch complexMolecular mechanismsPhosphorylated formMajor remodelingConformational changesMotive forceModel systemProteinBorrelia burgdorferiCheY3CheYMutantsTorque generatorFLIMInteractsCheXCW rotationMechanismRemodelingSubnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles
Li Z, Li W, Lu M, Bess J, Chao CW, Gorman J, Terry DS, Zhang B, Zhou T, Blanchard SC, Kwong PD, Lifson JD, Mothes W, Liu J. Subnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles. Nature Structural & Molecular Biology 2020, 27: 726-734. PMID: 32601441, PMCID: PMC8138683, DOI: 10.1038/s41594-020-0452-2.Peer-Reviewed Original ResearchAnalysis 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
Structural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography
Wang C, Tu J, Liu J, Molineux IJ. Structural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography. Nature Microbiology 2019, 4: 1049-1056. PMID: 30886360, PMCID: PMC6533119, DOI: 10.1038/s41564-019-0403-z.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyOuter membraneInfection initiationCell surfaceBacterial cell envelopeSalmonella enterica serovar TyphimuriumGenome translocationGram-negative bacteriaEnterica serovar TyphimuriumTail needleCytoplasmic membraneSecond proteinExtracellular channelsCell envelopePhage P22Successful infectionCell cytoplasmSerovar TyphimuriumSuch virionsGenomeCytoplasmProteinO-antigenPhagesAssembles
2018
A unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel
Chetrit D, Hu B, Christie PJ, Roy CR, Liu J. A unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel. Nature Microbiology 2018, 3: 678-686. PMID: 29784975, PMCID: PMC5970066, DOI: 10.1038/s41564-018-0165-z.Peer-Reviewed Original ResearchConceptsCytoplasmic complexType IV secretion channelType IV secretion systemInner membrane complexTranslocation of substratesCryo-electron tomographySecretion channelCell polesCytoplasmic ATPaseSecretion systemT4SS functionHexameric assemblyMembrane complexCytoplasmic channelsDNA complexesSubstrate transferT4SSChannel activationATPaseComplexesDistinct stagesAssemblyBiogenesisATPasesFurther analysis
2011
Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle
Luther PK, Winkler H, Taylor K, Zoghbi ME, Craig R, Padrón R, Squire JM, Liu J. Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 11423-11428. PMID: 21705660, PMCID: PMC3136262, DOI: 10.1073/pnas.1103216108.Peer-Reviewed Original Research
2010
Electron Tomography of Cryofixed, Isometrically Contracting Insect Flight Muscle Reveals Novel Actin-Myosin Interactions
Wu S, Liu J, Reedy MC, Tregear RT, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Goldman YE, Reedy MK, Taylor KA. Electron Tomography of Cryofixed, Isometrically Contracting Insect Flight Muscle Reveals Novel Actin-Myosin Interactions. PLOS ONE 2010, 5: e12643. PMID: 20844746, PMCID: PMC2936580, DOI: 10.1371/journal.pone.0012643.Peer-Reviewed Original Research
2008
The 3D Structure of Villin as an Unusual F-Actin Crosslinker
Hampton CM, Liu J, Taylor DW, DeRosier DJ, Taylor KA. The 3D Structure of Villin as an Unusual F-Actin Crosslinker. Structure 2008, 16: 1882-1891. PMID: 19081064, PMCID: PMC2782859, DOI: 10.1016/j.str.2008.09.015.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsBinding SitesChickensCross-Linking ReagentsImage Processing, Computer-AssistedImaging, Three-DimensionalIntestinesMicrofilament ProteinsModels, MolecularMolecular Sequence DataMolecular WeightMuscle, SkeletalProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRabbitsSequence Homology, Amino AcidIntegrin αIIbβ3 in a Membrane Environment Remains the Same Height after Mn2+ Activation when Observed by Cryoelectron Tomography
Ye F, Liu J, Winkler H, Taylor KA. Integrin αIIbβ3 in a Membrane Environment Remains the Same Height after Mn2+ Activation when Observed by Cryoelectron Tomography. Journal Of Molecular Biology 2008, 378: 976-986. PMID: 18405917, PMCID: PMC2614134, DOI: 10.1016/j.jmb.2008.03.014.Peer-Reviewed Original ResearchMeSH KeywordsCell MembraneHumansLiposomesManganeseModels, MolecularPlatelet Glycoprotein GPIIb-IIIa ComplexProtein ConformationTomography
2006
Electron Tomography of Swollen Rigor Fibers of Insect Flight Muscle Reveals a Short and Variably Angled S2 Domain
Liu J, Wu S, Reedy MC, Winkler H, Lucaveche C, Cheng Y, Reedy MK, Taylor KA. Electron Tomography of Swollen Rigor Fibers of Insect Flight Muscle Reveals a Short and Variably Angled S2 Domain. Journal Of Molecular Biology 2006, 362: 844-860. PMID: 16949613, DOI: 10.1016/j.jmb.2006.07.084.Peer-Reviewed Original Research