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
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 Specificity
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