2025
Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2
Koide E, Pietz H, Beltran J, Chen J. Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2. Nature Communications 2025, 16: 484. PMID: 39779684, PMCID: PMC11711199, DOI: 10.1038/s41467-024-55810-w.Peer-Reviewed Original ResearchConceptsAutoinhibited stateR domainPost-translocation stateSubstrate-binding sitePre-translocation stateATP-binding siteProtein 2Nucleotide-binding domain 2Cryogenic electron microscopyStructural basisDiverse array of compoundsDomain 2Cryo-EMRegulation mechanismChemotherapeutic resistanceConformational changesMultidrug resistanceArray of compoundsDiverse arrayConformational statesLiver homeostasisMultidrug resistance-associated protein 2Initial transportSubstrateCytosol
2022
Structures of the CcmABCD heme release complex at multiple states
Li J, Zheng W, Gu M, Han L, Luo Y, Yu K, Sun M, Zong Y, Ma X, Liu B, Lowder EP, Mendez DL, Kranz RG, Zhang K, Zhu J. Structures of the CcmABCD heme release complex at multiple states. Nature Communications 2022, 13: 6422. PMID: 36307425, PMCID: PMC9616876, DOI: 10.1038/s41467-022-34136-5.Peer-Reviewed Original ResearchConceptsHigh-resolution cryo-EM structuresResolution cryo-EM structureABC transporter complexAttachment of hemeCryo-EM structureLarge membrane complexesHeme-binding siteATP-binding siteATP-dependent releaseTransfer of hemeC-type cytochromesHeme chaperoneHeme traffickingCytochrome c proteinMembrane proteinsHeme transferTransporter complexMembrane complexATP hydrolysisStructural basisC proteinAMP-PNPFunctional studiesHeme releaseUnbound form
2021
Biochemical characterization of an E. coli cell division factor FtsE shows ATPase cycles similar to the NBDs of ABC-transporters
Mallick S, Kumar A, Dodia H, Alexander C, Vasudevan D, Beuria T. Biochemical characterization of an E. coli cell division factor FtsE shows ATPase cycles similar to the NBDs of ABC-transporters. Bioscience Reports 2021, 41: bsr20203034. PMID: 33320186, PMCID: PMC7791547, DOI: 10.1042/bsr20203034.Peer-Reviewed Original ResearchConceptsFtsEX complexPG hydrolysisABC transportersCytoplasmic loopBiochemical characterizationATPase cycleCouple ATP hydrolysisATP-binding siteATPase activityE. coliBacterial cell wallTransduce signalsInner membraneSequence similarityBacterial divisionSignal transductionPeptidoglycan layerMid cellATP hydrolysisCell wallSoluble expressionBiochemical propertiesFtsE.Direct interactionTransport molecules
2012
Assessing the range of kinase autoinhibition mechanisms in the insulin receptor family
Artim SC, Mendrola JM, Lemmon MA. Assessing the range of kinase autoinhibition mechanisms in the insulin receptor family. Biochemical Journal 2012, 448: 213-220. PMID: 22992069, PMCID: PMC3492919, DOI: 10.1042/bj20121365.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAntigens, CDCatalytic DomainCrystallography, X-RayEnzyme ActivationHumansIn Vitro TechniquesModels, MolecularMutationNeoplasmsProtein Structure, QuaternaryReceptor Tyrosine Kinase-like Orphan ReceptorsReceptor, InsulinReceptor, trkARecombinant Proteins
1994
Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
Kim S, Willison K, Horwich A. Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends In Biochemical Sciences 1994, 19: 543-548. PMID: 7846767, DOI: 10.1016/0968-0004(94)90058-2.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceBinding SitesBiological EvolutionChaperonin 60ChaperoninsConserved SequenceIntracellular Signaling Peptides and ProteinsMicrotubule-Associated ProteinsMolecular Sequence DataNuclear ProteinsPeptidesSequence Alignmentt-Complex Genome RegionUbiquitin-Protein LigasesCloning and mRNA Expression of Human Unconventional Myosin-IC A Homologue of Amoeboid Myosins-I With a Single IQ Motif and an SH3 Domain
Bement W, Wirth J, Mooseker M. Cloning and mRNA Expression of Human Unconventional Myosin-IC A Homologue of Amoeboid Myosins-I With a Single IQ Motif and an SH3 Domain. Journal Of Molecular Biology 1994, 243: 356-363. PMID: 7932763, DOI: 10.1006/jmbi.1994.1662.Peer-Reviewed Original ResearchConceptsSrc homology 3 domainSingle IQ motifIQ motifComplete deduced amino acid sequenceDeduced amino acid sequenceSingle open reading frameC-terminal tailOpen reading frameATP-binding siteAmino acid sequenceMembrane-binding sitesMultiple sequence alignmentNorthern blot analysisSH3 domainCDNA clonesReading frameAcid sequenceSequence alignmentMyosin IC
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