Fig. 2: Cryo-EM structure of CP-bound barbed ends. | Nature Communications

Fig. 2: Cryo-EM structure of CP-bound barbed ends.

From: A barbed end interference mechanism reveals how capping protein promotes nucleation in branched actin networks

Fig. 2

A Overview of the Cryo-EM map of capped F-actin. The density has been sharpened and denoised using deepEMhancer82 B Atomic model of CP bound to the barbed end. While the penultimate protomer interacts extensively with CP, the barbed end side of the terminal protomer is bound mostly by the β tentacle. We highlight the position of the bound small molecules. Actin subunits are labeled A0 to A3 starting from the terminal actin protomer. C The structure of WASP-bound G-actin51 (PDBID:2A3Z) was superimposed onto the terminal protomer of the complex. The β tentacle occupies the binding pocket that a WH2 domain would need to bind the terminal protomer. Actin monomers are shown as surface, while the tentacle and the WH2 helices are shown as cartoons.

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