2023
Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexes
2021
A pentameric protein ring with novel architecture is required for herpesviral packaging
Didychuk A, Gates S, Gardner M, Strong L, Martin A, Glaunsinger B. A pentameric protein ring with novel architecture is required for herpesviral packaging. ELife 2021, 10: e62261. PMID: 33554858, PMCID: PMC7889075, DOI: 10.7554/elife.62261.Peer-Reviewed Original ResearchConceptsViral genomeAccessory factorsBind double-stranded DNAPositively charged central channelContext of KSHV infectionDouble-stranded DNA virusesPositively charged residuesOncogenic herpesvirus Kaposi's sarcoma-associated herpesvirusKaposi's sarcoma-associated herpesvirusDouble-stranded DNASarcoma-associated herpesvirusGenome packagingHomologous proteinsNascent capsidsDNA bindingProtein ringGenomePackaging motorDNA virusesCharged residuesProgeny virionsMolecular motorsCentral channelKSHV infectionMutants
2015
Crystal structure of the eukaryotic origin recognition complex
Bleichert F, Botchan MR, Berger JM. Crystal structure of the eukaryotic origin recognition complex. Nature 2015, 519: 321-326. PMID: 25762138, PMCID: PMC4368505, DOI: 10.1038/nature14239.Peer-Reviewed Original ResearchConceptsOrigin recognition complexDrosophila origin recognition complexRecognition complexEukaryotic origin recognition complexHeterohexameric origin recognition complexMini-chromosome maintenance 2Winged-helix domainCatalytic amino acidsCellular DNA replicationWinged-helix foldORC subunitsEncircles DNAHelicase loadingGenomic integrityORC functionDevelopmental controlDNA replicationÅ resolutionDomain interactionsDisrupts interactionsCell cycleMaintenance 2Amino acidsCentral channelUnanticipated features
1999
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
Weber-Ban E, Reid B, Miranker A, Horwich A. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 1999, 401: 90-93. PMID: 10485712, DOI: 10.1038/43481.Peer-Reviewed Original ResearchConceptsSubstrate proteinsATP-dependent degradationGreen fluorescent protein GFPHydrogen exchange experimentsStable monomeric proteinFluorescent protein GFPNon-native formsChaperone ClpAChaperone familyEukaryotic proteinsProtease ClpPPresence of ATPChaperonin GroELHexameric ringClpAProteasome functionProtein GFPProtein structureMonomeric proteinNative proteinGlobal unfoldingProteinCentral channelRecognition peptideClpAP
1998
[11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL
Horwich A, Burston S, Rye H, Weissman J, Fenton W. [11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods In Enzymology 1998, 290: 141-146. PMID: 9534157, DOI: 10.1016/s0076-6879(98)90013-1.Peer-Reviewed Original ResearchConceptsBacterial chaperonin GroELGreen fluorescent proteinChaperonin GroELDouble-ring assemblyAddition of GroESDouble-ring complexesSingle-ring versionUnliganded GroELBacterial chaperoninsGroEL ringNeighboring subunitProtein foldsGroELEquatorial domainNonnative formsFluorescent proteinGroESNative stateNative formCentral channelCritical signalingSubunitsSignalingForm contactsNormal ATP
1997
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
Goldberg M, Zhang J, Sondek S, Matthews C, Fox R, Horwich A. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1080-1085. PMID: 9037009, PMCID: PMC19747, DOI: 10.1073/pnas.94.4.1080.Peer-Reviewed Original ResearchConceptsNative-like structureChaperonin GroELDihydrofolate reductaseProtein-folding intermediatesNative dihydrofolate reductaseStopped-flow fluorescence experimentsNonnative proteinsSubstrate proteinsProductive foldingPresence of ATPHuman dihydrofolate reductaseHydrogen-deuterium exchangeGroELPrimary structureProteinCentral channelHydrophobic interactionsFluorescence experimentsGroESFoldingSpeciesReductaseNMR spectroscopyDistant partsATP
1995
Unliganded GroEL at 2.8 Å: structure and functional implications
Sigler P, Horwich A. Unliganded GroEL at 2.8 Å: structure and functional implications. Philosophical Transactions Of The Royal Society B Biological Sciences 1995, 348: 113-119. PMID: 7770481, DOI: 10.1098/rstb.1995.0052.Peer-Reviewed Original ResearchConceptsATP-binding pocketCentral channelUnfolded polypeptidesApical domainThree-dimensional structureExtensive mutagenesisMutational studiesDyad symmetryC-terminusDistinct domainsGroELATP analogBiochemical studiesStructural scaffoldFunctional implicationsHigh saltSubunitsDomainChaperoninGroESMutagenesisEntire lengthCrystal formsPolypeptideSymmetric ring
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