2022
Structures of the CcmABCD heme release complex at multiple states
Li J, Zheng W, Gu M, Han L, Luo Y, Yu K, Sun M, Zong Y, Ma X, Liu B, Lowder EP, Mendez DL, Kranz RG, Zhang K, Zhu J. Structures of the CcmABCD heme release complex at multiple states. Nature Communications 2022, 13: 6422. PMID: 36307425, PMCID: PMC9616876, DOI: 10.1038/s41467-022-34136-5.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateBacterial Outer Membrane ProteinsBacterial ProteinsCytochromes cEscherichia coliEscherichia coli ProteinsHemeHemeproteinsConceptsHigh-resolution cryo-EM structuresResolution cryo-EM structureABC transporter complexAttachment of hemeCryo-EM structureLarge membrane complexesHeme-binding siteATP-binding siteATP-dependent releaseTransfer of hemeC-type cytochromesHeme chaperoneHeme traffickingCytochrome c proteinMembrane proteinsHeme transferTransporter complexMembrane complexATP hydrolysisStructural basisC proteinAMP-PNPFunctional studiesHeme releaseUnbound form
2021
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism
Rao Q, Han L, Wang Y, Chai P, Kuo YW, Yang R, Hu F, Yang Y, Howard J, Zhang K. Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism. Nature Structural & Molecular Biology 2021, 28: 799-810. PMID: 34556869, PMCID: PMC8500839, DOI: 10.1038/s41594-021-00656-9.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateCryoelectron MicroscopyDyneinsMicrotubulesModels, MolecularTetrahymena thermophilaConceptsOuter arm dyneinMicrotubule doubletsDistinct microtubule-binding domainsHigh-resolution structuresAction of dyneinsMicrotubule-binding domainNative tracksATP hydrolysisDynein motorsHydrolyze ATPConformational changesNucleotide cycleMotor coordination mechanismATP turnoverDyneinHead interactionsMechanical forces
2020
NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation
Leng F, Yin H, Qin S, Zhang K, Guan Y, Fang R, Wang H, Li G, Jiang Z, Sun F, Wang DC, Xie C. NLRP6 self-assembles into a linear molecular platform following LPS binding and ATP stimulation. Scientific Reports 2020, 10: 198. PMID: 31932628, PMCID: PMC6957519, DOI: 10.1038/s41598-019-57043-0.Peer-Reviewed Original ResearchConceptsNOD-like receptorsGlobal conformational changesStep-activation mechanismOuter membraneMolecular platformStructural basisAssembly patternsLigand specificityConformational changesInnate immune responseImmune receptorsActivation mechanismIntestinal homeostasisNegative bacteriaATP stimulationPathogen productsIntestinal tumorigenesisHigher molecular structuresMajor componentNLRP6Important roleHomodimerReceptorsCytosolImmune response
2013
Flexible 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
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