5YU8

Cofilin decorated actin filament

Summary for 5YU8

• Entry DOI: 10.2210/pdb5yu8/pdb
• EMDB information: 6844
• Descriptor: Actin, alpha skeletal muscle, Cofilin-2, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: actin, cofilin, cytosolic protein, muscle, cytoskeleton
• Biological source: Gallus gallus (Chicken); More
• Cellular location: Cytoplasm, cytoskeleton: P68139; Nucleus matrix : P21566
• Total number of polymer chains: 8
• Total formula weight: 267707.49

Authors

Tanaka, K.,Narita, A. (deposition date: 2017-11-21, release date: 2018-05-23, Last modification date: 2024-03-27)

Primary citation

Tanaka, K.,Takeda, S.,Mitsuoka, K.,Oda, T.,Kimura-Sakiyama, C.,Maeda, Y.,Narita, A.
Structural basis for cofilin binding and actin filament disassembly
Nat Commun, 9:1860-1860, 2018

PubMed Abstract: Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin (cofilin-decorated actin filament). The actin subunit structure of cofilactin (C-form) is distinct from those of F-actin (F-form) and monomeric actin (G-form). During the transition between these three conformations, the inner domain of actin (subdomains 3 and 4) and the majority of subdomain 1 move as two separate rigid bodies. The cofilin-actin interface consists of three distinct parts. Based on the rigid body movements of actin and the three cofilin-actin interfaces, we propose models for the cooperative binding of cofilin to actin, preferential binding of cofilin to ADP-bound actin filaments and cofilin-mediated severing of actin filaments.

PubMed: 29749375
DOI: 10.1038/s41467-018-04290-w

Experimental method

ELECTRON MICROSCOPY (3.8 Å)