EMD-10364

Single-particle
3.7 Å
EMD-10364 Deposition: 07/10/2019
Map released: 04/03/2020
Last modified: 02/12/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-10364

Cryo-EM structure of phalloidin-stabilized F-actin (aged)

EMD-10364

Single-particle
3.7 Å
EMD-10364 Deposition: 07/10/2019
Map released: 04/03/2020
Last modified: 02/12/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Rabbit, synthetic construct
Sample: Filamentous phalloidin-stabilized alpha actin in complex with ADP
Fitted models: 6t20 (Avg. Q-score: 0.446)

Deposition Authors: Pospich S, Merino F, Raunser S
Structural Effects and Functional Implications of Phalloidin and Jasplakinolide Binding to Actin Filaments.
Pospich S , Merino F , Raunser S
(2020) Structure , 28 , 437 - 449.e5
PUBMED: 32084355
DOI: doi:10.1016/j.str.2020.01.014
ISSN: 0969-2126
ASTM: STRUE6
Abstract:
Actin 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.