6t25
Cryo-EM structure of phalloidin-Alexa Flour-546-stabilized F-actin (copolymerized)Cryo-EM structure of phalloidin-Alexa Flour-546-stabilized F-actin (copolymerized)
Structural highlights
Function[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMedActin undergoes structural transitions during polymerization, ATP hydrolysis, and subsequent release of inorganic phosphate. Several actin-binding proteins sense specific states during this transition and can thus target different regions of the actin filament. Here, we show in atomic detail that phalloidin, a mushroom toxin that is routinely used to stabilize and label actin filaments, suspends the structural changes in actin, likely influencing its interaction with actin-binding proteins. Furthermore, high-resolution cryoelectron microscopy structures reveal structural rearrangements in F-actin upon inorganic phosphate release in phalloidin-stabilized filaments. We find that the effect of the sponge toxin jasplakinolide differs from the one of phalloidin, despite their overlapping binding site and similar interactions with the actin filament. Analysis of structural conformations of F-actin suggests that stabilizing agents trap states within the natural conformational space of actin. Structural Effects and Functional Implications of Phalloidin and Jasplakinolide Binding to Actin Filaments.,Pospich S, Merino F, Raunser S Structure. 2020 Feb 12. pii: S0969-2126(20)30041-1. doi:, 10.1016/j.str.2020.01.014. PMID:32084355[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| |||||||||||||||||||