Regular ArticleSmall Angle X-Ray Scattering and Electron Cryomicroscopy Study of Actin Filaments: Role of the Bound Nucleotide in the Structure of F-Actin
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The Connection Between Actin ATPase and Polymerization
2006, Advances in Molecular and Cell BiologyCitation Excerpt :Consequently, structural transitions in actin that accelerate ATP hydrolysis also remain to be elucidated. Cryoelectron microscopy has demonstrated that there is a structural difference between ATP/ADP·Pi filaments and ADP‐containing filaments, where the latter, that is, the ground state, has the most well‐ordered structure (Lepault et al., 1994). A difference between newly formed actin polymers, presumably consisting of ATP/ADP·Pi‐actin and filaments consisting of ADP‐actin, is further demonstrated by preferential binding of the filament‐nucleating Arp2/3 complex to the former in vitro (Ichetovkin et al., 2002).
Pure F-actin networks are distorted and branched by steps in the critical-point drying method
2002, Journal of Structural BiologyThe role of MeH73 in actin polymerization and ATP hydrolysis
2002, Journal of Molecular BiologyCitation Excerpt :At low salt concentrations, where the protein exists as monomers in solution, the nucleotide stabilizes the protein. Furthermore, nucleotide hydrolysis and Pi-release during polymerization have been implied to influence the final structure of the filament formed4–6. Hydrolysis of ATP on actin and product release might also be intrinsic to force generation during muscle contraction and non-muscle cell motility7,8.