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 ResearchMeSH KeywordsCryoelectron MicroscopyEndoplasmic Reticulum-Associated DegradationHydrophobic and Hydrophilic InteractionsMembrane GlycoproteinsModels, MolecularProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases