2024
High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations
Xu X, Cao W, Swift M, Pandit N, Huehn A, Sindelar C, De La Cruz E, Hanein D, Volkmann N. High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations. Communications Chemistry 2024, 7: 164. PMID: 39079963, PMCID: PMC11289367, DOI: 10.1038/s42004-024-01243-x.Peer-Reviewed Original ResearchActin filamentsVertebrate actinsActin structuresDNase I binding loopActin filament assemblyEukaryotic cell functionStructures of wild-typeNear-atomic resolution structuresPotential binding sitesActin subunitsFilament assemblyRegulatory proteinsDNase IA167ActinAdjacent subunitsRegulatory roleMolecular mechanismsVertebratesWild-typeGlutamic acidCell functionFilamentsSubunitResidues
2019
Bile Salts Alter the Mouse Norovirus Capsid Conformation: Possible Implications for Cell Attachment and Immune Evasion
Sherman MB, Williams AN, Smith HQ, Nelson C, Wilen CB, Fremont DH, Virgin HW, Smith TJ. Bile Salts Alter the Mouse Norovirus Capsid Conformation: Possible Implications for Cell Attachment and Immune Evasion. Journal Of Virology 2019, 93: 10.1128/jvi.00970-19. PMID: 31341042, PMCID: PMC6744230, DOI: 10.1128/jvi.00970-19.Peer-Reviewed Original ResearchConceptsCryo-EM structureP domainCryo-electron microscopy structureHigh-resolution cryo-EM structuresConformational changesImportant biological rolesSmall conformational changesMicroscopy structureHuman Norwalk virusCell attachmentAdjacent subunitsBiological roleIcosahedral capsidCapsid shellRNA virusesCapsid proteinBinding sitesIntrinsic affinityReceptor binding sitesCapsid conformationUnusual structureImmune evasionShell domainTarget cellsReceptorsMechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides
Chou SZ, Pollard TD. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 4265-4274. PMID: 30760599, PMCID: PMC6410863, DOI: 10.1073/pnas.1807028115.Peer-Reviewed Original ResearchConceptsATP hydrolysisActin filamentsBarbed endsMultiple favorable interactionsCryo-electron microscopyNetwork of interactionsShort-pitch helixActin polymerizationC-terminusAdjacent subunitsSubdomain 2Conformational changesEM structuresBinding loopSubdomain 3SubunitsPhosphate dissociationPointed endRelease sitesFilamentsActive siteConformationADPBackbone conformationSide chains
2016
Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits
Hocky GM, Baker JL, Bradley MJ, Sinitskiy AV, De La Cruz EM, Voth GA. Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits. The Journal Of Physical Chemistry B 2016, 120: 4558-4567. PMID: 27146246, PMCID: PMC4959277, DOI: 10.1021/acs.jpcb.6b02741.Peer-Reviewed Original ResearchConceptsActin filamentsRegulatory proteinsD-loopSite-specific mutagenesisSpecific divalent cationsFilament severingStructural bioinformaticsAdjacent subunitsAccessible conformational spaceSubunit conformationActin subunitsKey structural elementsAmino acidsLarge-scale changesConformational spaceSubunitsFilament mechanical propertiesProteinFilamentsDivalent cationsMagnesium ionsMolecular dynamics simulationsConformationSitesCofilin
2013
Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism*
Murray DS, Chinnam N, Tonthat NK, Whitfill T, Wray LV, Fisher SH, Schumacher MA. Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism*. Journal Of Biological Chemistry 2013, 288: 35801-35811. PMID: 24158439, PMCID: PMC3861631, DOI: 10.1074/jbc.m113.519496.Peer-Reviewed Original ResearchConceptsGlutamine synthetaseCatalytic conformational changesSpecific regulatory networksActive site constructionFeedback inhibition mechanismFeedback inhibitionGS isoenzymesCatalytic glutamateActive site reorganizationRegulatory networksEnzyme active siteNitrogen metabolismProduction of glutamineSpecific residuesAdjacent subunitsRegulatory mechanismsInhibitor designConformational changesConformational alterationsGram-positive pathogensCellular studiesEssential roleActive siteRegulatory stateGln
2012
Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness
Kang H, Bradley MJ, McCullough BR, Pierre A, Grintsevich EE, Reisler E, De La Cruz EM. Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16923-16927. PMID: 23027950, PMCID: PMC3479481, DOI: 10.1073/pnas.1211078109.Peer-Reviewed Original ResearchConceptsCation-binding sitesActin assemblyEukaryotic biologyLong-pitch helixActin functionSalt-dependent effectsCell divisionCell motilityActin polymerizationFilament assemblyAdjacent subunitsIntracellular transportActin filamentsPhysiological salt concentrationsActin monomersCellular shapeNonspecific ionic strength effectsDiscrete sites
2002
Monomeric Yeast PCNA Mutants Are Defective in Interacting with and Stimulating the ATPase Activity of RFC †
Ionescu CN, Shea KA, Mehra R, Prundeanu L, McAlear MA. Monomeric Yeast PCNA Mutants Are Defective in Interacting with and Stimulating the ATPase Activity of RFC †. Biochemistry 2002, 41: 12975-12985. PMID: 12390024, DOI: 10.1021/bi026029s.Peer-Reviewed Original ResearchConceptsReplication factor CMutant PCNAsDNA clampDNA damaging agent methylmethane sulfonateDNA polymerase accessory proteinMutant PCNA proteinsAgent methylmethane sulfonatePolymerase accessory proteinsProtein-protein interactionsWild-type subunitsSingle amino acid substitutionDNA repair pathwaysATPase activityE. coliAmino acid substitutionsYeast PCNAPCNA mutantsClamp loaderPCNA functionPCNA trimerBeta clampAccessory proteinsRepair pathwaysMethylmethane sulfonateAdjacent subunits
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