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 SpecificityFlexible interwoven termini determine the thermal stability of thermosomes
Zhang K, Wang L, Liu Y, Chan KY, Pang X, Schulten K, Dong Z, Sun F. Flexible interwoven termini determine the thermal stability of thermosomes. Protein & Cell 2013, 4: 432-444. PMID: 23709365, PMCID: PMC3740188, DOI: 10.1007/s13238-013-3026-9.Peer-Reviewed Original Research
2010
Five mutations in N-terminus confer thermostability on mesophilic xylanase
Zhang S, Zhang K, Chen X, Chu X, Sun F, Dong Z. Five mutations in N-terminus confer thermostability on mesophilic xylanase. Biochemical And Biophysical Research Communications 2010, 395: 200-206. PMID: 20361933, DOI: 10.1016/j.bbrc.2010.03.159.Peer-Reviewed Original Research