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
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 ResearchConceptsN-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 structureAtomic 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
Cryo-EM structure of a transcribing cypovirus
Yang C, Ji G, Liu H, Zhang K, Liu G, Sun F, Zhu P, Cheng L. Cryo-EM structure of a transcribing cypovirus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 6118-6123. PMID: 22492979, PMCID: PMC3341035, DOI: 10.1073/pnas.1200206109.Peer-Reviewed Original ResearchMeSH KeywordsCapsidCapsid ProteinsCryoelectron MicroscopyModels, MolecularProtein ConformationProtein Structure, TertiaryReoviridaeRNA, MessengerRNA, ViralTranscription, GeneticConceptsNascent mRNATurret proteinFamily ReoviridaeCapsid shellConformational changesCapsid proteinMRNA transcriptionCryo-EM structureMajor capsid proteinGood model systemGuanylyltransferase domainTranscription cycleViral capsid proteinsIcosahedral viral capsidsCypovirusGenomic RNACryoelectron microscopyGMP moietyRNA virusesProteinViral capsidTranscriptionMRNAReoviridaeModel system
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 ResearchAutotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore
Zhai Y, Zhang K, Huo Y, Zhu Y, Zhou Q, Lu J, Black I, Pang X, Roszak AW, Zhang X, Isaacs NW, Sun F. Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore. Biochemical Journal 2011, 435: 577-587. PMID: 21306302, DOI: 10.1042/bj20101548.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
2010
Crystal Structure of Group II Chaperonin in the Open State
Huo Y, Hu Z, Zhang K, Wang L, Zhai Y, Zhou Q, Lander G, Zhu J, He Y, Pang X, Xu W, Bartlam M, Dong Z, Sun F. Crystal Structure of Group II Chaperonin in the Open State. Structure 2010, 18: 1270-1279. PMID: 20947016, PMCID: PMC3048791, DOI: 10.1016/j.str.2010.07.009.Peer-Reviewed Original ResearchConceptsGroup II chaperoninLid domainConformational changesOpen stateATP-dependent mannerHigh-resolution structuresDetailed conformational changesFunctional cycleThermosomeHydrophobic patchStructural comparisonProtease K digestionChaperoninClosed stateK digestionCrystal structureStructural fittingOpen formComplete crystal structureClosed structureSpeciesDomainProteinATPElectron microscopy