2019
New interfaces on MiD51 for Drp1 recruitment and regulation
Ma J, Zhai Y, Chen M, Zhang K, Chen Q, Pang X, Sun F. New interfaces on MiD51 for Drp1 recruitment and regulation. PLOS ONE 2019, 14: e0211459. PMID: 30703167, PMCID: PMC6355003, DOI: 10.1371/journal.pone.0211459.Peer-Reviewed Original Research
2017
Crystal structure of E. coli apolipoprotein N-acyl transferase
Lu G, Xu Y, Zhang K, Xiong Y, Li H, Cui L, Wang X, Lou J, Zhai Y, Sun F, Zhang XC. Crystal structure of E. coli apolipoprotein N-acyl transferase. Nature Communications 2017, 8: 15948. PMID: 28885614, PMCID: PMC5500890, DOI: 10.1038/ncomms15948.Peer-Reviewed Original ResearchConceptsApolipoprotein N-acyl transferaseN-acyl transferaseTM domainN-terminal cysteine residueThree-step pathwayGram-negative bacteriaLid loopTransmembrane domainPeriplasmic sideTM helicesCysteine residuesLipid modificationLipid donorCatalytic cavityAcceptor substrateLipid bilayersLipid leafletCatalytic centerAcyl chainsCrystal structurePathwayTransferaseLateral openingDomainProtein
2014
C-terminal motif within Sec7 domain regulates guanine nucleotide exchange activity via tuning protein conformation
Qiu B, Zhang K, Wang S, Sun F. C-terminal motif within Sec7 domain regulates guanine nucleotide exchange activity via tuning protein conformation. Biochemical And Biophysical Research Communications 2014, 446: 380-386. PMID: 24613384, DOI: 10.1016/j.bbrc.2014.02.125.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceBinding SitesConserved SequenceCrystallography, X-RayGuanine Nucleotide Exchange FactorsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein StabilityProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidStatic ElectricityStructural Homology, ProteinConceptsGuanine exchange factorSec7 domainARF-GEFCatalytic domainActivity regulationGolgi network membranesNucleotide exchange activityC-terminal motifGEF catalytic activityADP-ribosylation factorCatalytic activity regulationExchange activityActivation of ARFARF-GEFsMembrane trafficExchange factorHelix JOrganelle structureMolecular detailsMutagenesis studiesProtein conformationLoop regionMotifRegulationKey role
2013
Structure Reveals Regulatory Mechanisms of a MaoC-Like Hydratase from Phytophthora capsici Involved in Biosynthesis of Polyhydroxyalkanoates (PHAs)
Wang H, Zhang K, Zhu J, Song W, Zhao L, Zhang X. Structure Reveals Regulatory Mechanisms of a MaoC-Like Hydratase from Phytophthora capsici Involved in Biosynthesis of Polyhydroxyalkanoates (PHAs). PLOS ONE 2013, 8: e80024. PMID: 24244597, PMCID: PMC3823801, DOI: 10.1371/journal.pone.0080024.Peer-Reviewed Original ResearchAcyl Coenzyme AAmino Acid SequenceBinding SitesBiocatalysisCatalytic DomainCrystallography, X-RayEnoyl-CoA HydrataseEscherichia coliModels, MolecularMolecular Sequence DataMutationOxidation-ReductionPhytophthoraPolyhydroxyalkanoatesProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidSubstrate SpecificityIdentification of SERPINB1 As a Physiological Inhibitor of Human Granzyme H
Wang L, Li Q, Wu L, Liu S, Zhang Y, Yang X, Zhu P, Zhang H, Zhang K, Lou J, Liu P, Tong L, Sun F, Fan Z. Identification of SERPINB1 As a Physiological Inhibitor of Human Granzyme H. The Journal Of Immunology 2013, 190: 1319-1330. PMID: 23269243, DOI: 10.4049/jimmunol.1202542.Peer-Reviewed Original ResearchCatalysisCell Line, TumorChromatography, GelCrystallography, X-RayCytoplasmic GranulesCytotoxicity, ImmunologicGenetic VectorsGranzymesHumansJurkat CellsKiller Cells, Lymphokine-ActivatedModels, MolecularNeoplasm ProteinsProtein BindingProtein ConformationProtein Interaction MappingRecombinant Fusion ProteinsSerpinsStructure-Activity RelationshipAtomic Model of Rabbit Hemorrhagic Disease Virus by Cryo-Electron Microscopy and Crystallography
Wang X, Xu F, Liu J, Gao B, Liu Y, Zhai Y, Ma J, Zhang K, Baker TS, Schulten K, Zheng D, Pang H, Sun F. Atomic Model of Rabbit Hemorrhagic Disease Virus by Cryo-Electron Microscopy and Crystallography. PLOS Pathogens 2013, 9: e1003132. PMID: 23341770, PMCID: PMC3547835, DOI: 10.1371/journal.ppat.1003132.Peer-Reviewed Original Research
2012
Structural Insights into the Substrate Specificity of Human Granzyme H: The Functional Roles of a Novel RKR Motif
Wang L, Zhang K, Wu L, Liu S, Zhang H, Zhou Q, Tong L, Sun F, Fan Z. Structural Insights into the Substrate Specificity of Human Granzyme H: The Functional Roles of a Novel RKR Motif. The Journal Of Immunology 2012, 188: 765-773. PMID: 22156497, DOI: 10.4049/jimmunol.1101381.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsCatalytic DomainCatsCell LineCell Line, TransformedCrystallography, X-RayCytotoxicity, ImmunologicDogsGranzymesHumansHydrogen-Ion ConcentrationK562 CellsMolecular Sequence DataPan troglodytesProtein BindingSerine Proteinase InhibitorsSubstrate SpecificityConceptsRKR motifHuman granzyme HStructural insightsSubstrate recognition mechanismChymotrypsin-like serine proteaseGranzyme HSubstrate recognitionSubstrate specificitySubstrate preferenceChloromethylketone inhibitorAcidic residuesInnate immune responseAromatic residuesFunctional roleP1 positionSerine proteasesS1 pocketRecognition mechanismMotifGzmHResiduesProteolytic activityDecapeptide substrateImportant roleMutants
2011
Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis
Zheng X, Guo J, Xu L, Li H, Zhang D, Zhang K, Sun F, Wen T, Liu S, Pang H. Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis. PLOS ONE 2011, 6: e20506. PMID: 21637775, PMCID: PMC3102732, DOI: 10.1371/journal.pone.0020506.Peer-Reviewed Original Research