2017
Structural basis of MsbA-mediated lipopolysaccharide transport
Mi W, Li Y, Yoon SH, Ernst RK, Walz T, Liao M. Structural basis of MsbA-mediated lipopolysaccharide transport. Nature 2017, 549: 233-237. PMID: 28869968, PMCID: PMC5759761, DOI: 10.1038/nature23649.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine DiphosphateATP-Binding Cassette TransportersBacterial ProteinsBiological TransportCell MembraneCryoelectron MicroscopyEscherichia coliHydrophobic and Hydrophilic InteractionsLipid BilayersLipopolysaccharidesModels, MolecularNanostructuresPeriplasmProtein BindingProtein DomainsConceptsPeriplasmic leafletStructural basisSingle-particle cryo-electron microscopyCryo-electron microscopyÅ resolution structureLipid flippasesGram-negative bacteriaLipopolysaccharide transportTransmembrane domainInner membraneCytoplasmic leafletMsbAOuter membraneCell envelopeResolution structureCassette transportersADP-vanadateStructural mechanismsConformational transitionLPS recognitionFunctional stateFlippasesMsbA.Hydrophobic interactionsMembraneCryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3
Schoebel S, Mi W, Stein A, Ovchinnikov S, Pavlovicz R, DiMaio F, Baker D, Chambers MG, Su H, Li D, Rapoport TA, Liao M. Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3. Nature 2017, 548: 352-355. PMID: 28682307, PMCID: PMC5736104, DOI: 10.1038/nature23314.Peer-Reviewed Original Research
2009
CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy
Meng X, Wang G, Viero C, Wang Q, Mi W, Su XD, Wagenknecht T, Williams AJ, Liu Z, Yin CC. CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy. Journal Of Molecular Biology 2009, 387: 320-334. PMID: 19356589, PMCID: PMC2667806, DOI: 10.1016/j.jmb.2009.01.059.Peer-Reviewed Original ResearchConceptsCryo-electron microscopyChannel activitySkeletal ryanodine receptorsAffinity of ryanodineSkeletal sarcoplasmic reticulum vesiclesSmall proteinsClamp regionConformational changesPhysiological functionsDomain 5Closed stateSingle-channel recordingsStructural familyRyR1 channelsRyanodine receptorSkeletal muscleRyR1VesiclesOpen probabilityRyR channelsChannel 2Channel recordingsEfflux rateSarcoplasmic reticulum vesiclesReticulum vesicles