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
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