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 formThe SpoVA membrane complex is required for dipicolinic acid import during sporulation and export during germination
Gao Y, Barajas-Ornelas R, Amon J, Ramírez-Guadiana F, Alon A, Brock K, Marks D, Kruse A, Rudner D. The SpoVA membrane complex is required for dipicolinic acid import during sporulation and export during germination. Genes & Development 2022, 36: 634-646. PMID: 35654455, PMCID: PMC9186386, DOI: 10.1101/gad.349488.122.Peer-Reviewed Original ResearchConceptsMembrane complexStress-resistant sporesEndospore-forming bacteriaResponse to starvationDipicolinic acidEB subunitsDPA releaseCytoplasmic plugIn vivo analysisMembrane channelsStress resistanceD subunitDormant sporesMolecular basisResume growthSporulationNutrient detectionSporesGerminationProteinOperonSpoVAMutagenesisLociMembrane
2020
In Situ Structure of the Vibrio Polar Flagellum Reveals a Distinct Outer Membrane Complex and Its Specific Interaction with the Stator
Zhu S, Nishikino T, Takekawa N, Terashima H, Kojima S, Imada K, Homma M, Liu J. In Situ Structure of the Vibrio Polar Flagellum Reveals a Distinct Outer Membrane Complex and Its Specific Interaction with the Stator. Journal Of Bacteriology 2020, 202: 10.1128/jb.00592-19. PMID: 31767780, PMCID: PMC6989802, DOI: 10.1128/jb.00592-19.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsCryo-electron tomographyStator unitsFlagellar rotationDetailed protein-protein interactionsUnique protein-protein interactionsGram-negative marine bacteriumPolar sheathed flagellumBasal body structureHigh-speed motilityBacterial flagellar motorLarge conformational changesSpecific interactionsFirst structural evidencePeriplasmic domainPolar flagellumFlagellar motorPeptidoglycan layerMembrane complexT ringMarine bacteriumBacterial flagellaGenetic analysisDetailed structural informationSheathed flagellum
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
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
2015
Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40*
Kuszak A, Jacobs D, Gurnev P, Shiota T, Louis J, Lithgow T, Bezrukov S, Rostovtseva T, Buchanan S. Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40*. Journal Of Biological Chemistry 2015, 290: 26204-26217. PMID: 26336107, PMCID: PMC4646270, DOI: 10.1074/jbc.m115.642173.Peer-Reviewed Original ResearchConceptsC-terminal domainPresequence peptideC-terminusMitochondrial outer membraneAmino acidsΒ-barrel domainYeast Candida glabrataOuter membrane complexSubstrate Binding AffinityTranslocase complexNuclear genomeTom40 proteinMitochondrial proteinsProtein transportTom40Substrate recognitionHelical domainOuter membraneMembrane complexCentral subunitN-terminusPlanar lipid membranesTransport functionTerminusChannel conformation
1990
The "microassembly" of integral membrane proteins: applications & implications.
Popot J, Engelman D, Zaccai G, de Vitry C. The "microassembly" of integral membrane proteins: applications & implications. Progress In Clinical And Biological Research 1990, 343: 237-62. PMID: 2198582.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsFunctional integral membrane proteinsMost integral membrane proteinsSingle transmembrane alpha-helixInner membrane complexTransmembrane alpha-helixAutonomous folding domainsInner membraneIntegral subunitThree-dimensional structureTransmembrane regionSequence dataMembrane complexAlpha-helixExtensive rearrangementTertiary structureProteinPolypeptideLipid phasePossible roleOrganellesBiosynthesisSubunitsLocal interactions
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