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 ResearchMeSH KeywordsAdenosine TriphosphateBacterial Outer Membrane ProteinsBacterial ProteinsCytochromes cEscherichia coliEscherichia coli ProteinsHemeHemeproteinsConceptsHigh-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 form
2021
Cryo-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 ResearchMeSH KeywordsBinding SitesCryoelectron MicroscopyCytochrome b GroupEscherichia coliEscherichia coli ProteinsHemeOxidation-ReductionPhospholipidsProtein ConformationProton PumpsUbiquinoneConceptsHydrogen 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 study
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