Shuhui Wang
Associate Research ScientistAbout
Research
Publications
2025
Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.
Wang S, Brischigliaro M, Zhang Y, Wu C, Zheng W, Barrientos A, Xiong Y. Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation. BioRxiv 2025 PMID: 41446151, DOI: 10.64898/2025.12.18.695269.Peer-Reviewed Original Research In PressVisualizing the translation landscape in human cells at high resolution
Zheng W, Zhang Y, Wang J, Wang S, Chai P, Bailey E, Zhu C, Guo W, Devarkar S, Wu S, Lin J, Zhang K, Liu J, Lomakin I, Xiong Y. Visualizing the translation landscape in human cells at high resolution. Nature Communications 2025, 16: 10757. PMID: 41315256, PMCID: PMC12663405, DOI: 10.1038/s41467-025-65795-9.Peer-Reviewed Original ResearchConceptsTranslational landscapeHuman cellsCryo-focused ion beamHigh-resolution structuresHuman 80S ribosomesSingle-particle cryo-electron microscopyCryo-EM approachCryo-electron microscopyRibosome structurePurified ribosomesConsensus structureRibosomeE siteA-resolutionIon beamCryo-EMProtein synthesisNative ribosomesStructure of macromoleculesNative environmentPolyamine bindingCycloheximideEnvironment of ionsCellsPolyamines
2024
Structures of the Mycobacterium tuberculosis efflux pump EfpA reveal the mechanisms of transport and inhibition
Wang S, Wang K, Song K, Lai Z, Li P, Li D, Sun Y, Mei Y, Xu C, Liao M. Structures of the Mycobacterium tuberculosis efflux pump EfpA reveal the mechanisms of transport and inhibition. Nature Communications 2024, 15: 7710. PMID: 39231991, PMCID: PMC11375168, DOI: 10.1038/s41467-024-51948-9.Peer-Reviewed Original ResearchConceptsCryo-EM structureMultidrug efflux pumpsLipid binding sitesOutward-open conformationLipid flippasesLipid bindingEfflux pumpsInner membrane leafletInward-openInner leafletOuter leafletDrug targetsBinding sitesMembrane leafletLipid siteMycobacterium tuberculosisMechanism of transportMycobacteriaLipidOverall structureEFPAEndogenous lipidsAnti-TB drugsInhibitory mechanismFlippase
2023
The structure of phosphatidylinositol remodeling MBOAT7 reveals its catalytic mechanism and enables inhibitor identification
Wang K, Lee C, Sui X, Kim S, Wang S, Higgs A, Baublis A, Voth G, Liao M, Walther T, Farese R. The structure of phosphatidylinositol remodeling MBOAT7 reveals its catalytic mechanism and enables inhibitor identification. Nature Communications 2023, 14: 3533. PMID: 37316513, PMCID: PMC10267149, DOI: 10.1038/s41467-023-38932-5.Peer-Reviewed Original ResearchConceptsCatalytic mechanismER lumenal sideIdentification of small molecule inhibitorsN-terminal residuesLumen sideEnzyme specificitySmall molecule inhibitorsSubstrate selectivityLands cycleInhibitor identificationCatalytic centerVirtual screeningMBOAT7Lyso-phosphatidylinositolLyso-PILyso-phospholipidsBrain developmental disorderLead compoundsAcyl chainsMBOATFatty liver diseaseExpressionCytosolMutationsPharmacological development
2020
Structural insights into substrate recognition by the type VII secretion system.
Wang S, Zhou K, Yang X, Zhang B, Zhao Y, Xiao Y, Yang X, Yang H, Guddat LW, Li J, Rao Z. Structural insights into substrate recognition by the type VII secretion system. Protein Cell 2020, 11: 124-137. PMID: 31758528, DOI: 10.1007/s13238-019-00671-z.Peer-Reviewed Original Research
2018
An electron transfer path connects subunits of a mycobacterial respiratory supercomplex.
Gong H, Li J, Xu A, Tang Y, Ji W, Gao R, Wang S, Yu L, Tian C, Li J, Yen HY, Man Lam S, Shui G, Yang X, Sun Y, Li X, Jia M, Yang C, Jiang B, Lou Z, Robinson CV, Wong LL, Guddat LW, Sun F, Wang Q, Rao Z. An electron transfer path connects subunits of a mycobacterial respiratory supercomplex. Science 2018, 362 PMID: 30361386, DOI: 10.1126/science.aat8923.Peer-Reviewed Original Research
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Molecular Biophysics and Biochemistry
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