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 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 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
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