2022
The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation
Tachiyama S, Chan KL, Liu X, Hathroubi S, Li W, Peterson B, Khan M, Ottemann K, Liu J, Roujeinikova A. The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2118401119. PMID: 35046042, PMCID: PMC8794807, DOI: 10.1073/pnas.2118401119.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial Physiological PhenomenaBacterial ProteinsFlagellaHelicobacter pyloriMembrane ProteinsModels, MolecularMolecular Motor ProteinsMultiprotein ComplexesProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein TransportStructure-Activity RelationshipConceptsStator unitsStomatin/prohibitin/flotillin/HflK/C (SPFH) domainWild-type cellsSignificant structural similarityPeriplasmic domainAssembly factorsFlagellar motorAccessory proteinsFliLLinker regionActive conformationFlagellar baseC-domainMotBStructural similarityStator assemblyProteinPutative mechanismsElectron tomography reconstructionsIntact motorCellsActivationDomainMotAHelix
2020
Subnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles
Li Z, Li W, Lu M, Bess J, Chao CW, Gorman J, Terry DS, Zhang B, Zhou T, Blanchard SC, Kwong PD, Lifson JD, Mothes W, Liu J. Subnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles. Nature Structural & Molecular Biology 2020, 27: 726-734. PMID: 32601441, PMCID: PMC8138683, DOI: 10.1038/s41594-020-0452-2.Peer-Reviewed Original Research