6RSW
HFD domain of mouse CAP1 bound to the pointed end of G-actin
Summary for 6RSW
| Entry DOI | 10.2210/pdb6rsw/pdb |
| Related | 6RSQ |
| Descriptor | Actin, alpha skeletal muscle, Twinfilin-1, Adenylyl cyclase-associated protein 1, ... (7 entities in total) |
| Functional Keywords | actin binding protein, contractile protein |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 3 |
| Total formula weight | 78703.97 |
| Authors | Kotila, T.,Kogan, K.,Lappalainen, P. (deposition date: 2019-05-22, release date: 2019-11-27, Last modification date: 2024-01-24) |
| Primary citation | Kotila, T.,Wioland, H.,Enkavi, G.,Kogan, K.,Vattulainen, I.,Jegou, A.,Romet-Lemonne, G.,Lappalainen, P. Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Nat Commun, 10:5320-5320, 2019 Cited by PubMed Abstract: The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes. PubMed: 31757941DOI: 10.1038/s41467-019-13213-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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