2015
The structure of the dynactin complex and its interaction with dynein
Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP. The structure of the dynactin complex and its interaction with dynein. Science 2015, 347: 1441-1446. PMID: 25814576, PMCID: PMC4413427, DOI: 10.1126/science.aaa4080.Peer-Reviewed Original ResearchConceptsDynactin complexBicaudal D2Microtubule motors cytoplasmic dynein-1Distinct protein complexesCytoplasmic dynein-1Cryo-electron microscopyProtein Arp1Protein complexesAngstrom structureDynein 1DynactinEssential cofactorΒ-actinDyneinShoulder domainDependent interactionFilamentsComplexesArp1CofactorActinCopiesInteractionPeptidesDomain
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 SpecificityStructural Insights into the Intrinsic Self-Assembly of Par-3 N-Terminal Domain
Zhang Y, Wang W, Chen J, Zhang K, Gao F, Gao B, Zhang S, Dong M, Besenbacher F, Gong W, Zhang M, Sun F, Feng W. Structural Insights into the Intrinsic Self-Assembly of Par-3 N-Terminal Domain. Structure 2013, 21: 997-1006. PMID: 23643951, DOI: 10.1016/j.str.2013.04.004.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingCell Cycle ProteinsCryoelectron MicroscopyMembrane ProteinsMicroscopy, Atomic ForceModels, MolecularProtein Structure, SecondaryProtein Structure, TertiaryConceptsN-terminal domainPAR-3PAR-3/PARCell polarity establishmentPolarity establishmentEpithelial polarizationScaffold proteinProtein domainsLongitudinal packingStructural basisStructural insightsCryoelectron microscopyCentral organizerFilament-like structuresC complexFilament structureSelf-association capacitySelf-associationUnderlying mechanismDomainElectrostatic interactionsInteraction modesProteinCrystal structure
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 ResearchAtomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping
Cheng L, Sun J, Zhang K, Mou Z, Huang X, Ji G, Sun F, Zhang J, Zhu P. Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 1373-1378. PMID: 21220303, PMCID: PMC3029759, DOI: 10.1073/pnas.1014995108.Peer-Reviewed Original ResearchConceptsCytoplasmic polyhedrosis virusDeduced amino acid sequenceCryo-EM structureRNA segment 7Amino acid sequenceMechanisms of mRNANascent mRNAEnzymatic domainsAcid sequenceCryoelectron microscopyFamily ReoviridaeProtein VP5Capsid shellPolyhedrosis virusFull atomic modelsAtomic modelStructural organizationGuanylyltransferaseMRNASegment 7ProteinCypovirus