9Q7M
Barbed end of cofilin actin, cofilin on second-to-last barbed end subunit
Summary for 9Q7M
| Entry DOI | 10.2210/pdb9q7m/pdb |
| EMDB information | 72307 |
| Descriptor | Actin, alpha skeletal muscle, Cofilin-2, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | cytoskeleton, actin, filament, helical, protein fibril |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 9 |
| Total formula weight | 287213.90 |
| Authors | Palmer, N.J.,Dominguez, R. (deposition date: 2025-08-24, release date: 2026-03-04, Last modification date: 2026-05-13) |
| Primary citation | Palmer, N.J.,Boczkowska, M.,Rebowski, G.,Dominguez, R. Mechanisms of disassembly at the actin filament pointed and barbed ends. Sci Adv, 12:eaee5882-eaee5882, 2026 Cited by PubMed Abstract: Actin cytoskeleton dynamics power processes from cell motility to organelle trafficking, requiring rapid polymerization and depolymerization accelerated in cells by regulatory proteins. While mechanisms of accelerated polymerization are relatively well studied, those of depolymerization remain poorly understood. Here, we present twelve cryo-electron microscopy structures showing how cofilin, cyclase-associated protein (CAP), and capping protein (CP) coordinate their activities to accelerate depolymerization at both filament ends. Alone, CAP produces a ~4.0 Å lateral displacement of the first pointed-end subunit, whereas cofilin reverts terminal subunits at the pointed and barbed ends to a G-actin-like conformation and undertwists the filament short-pitch helix. When functioning together, these cofilin- and CAP-induced conformational changes are amplified to accelerate pointed-end disassembly. At the barbed end, the cofilin-induced changes trigger stepwise CP dissociation and favor depolymerization. These findings support end-specific mechanisms of filament disassembly through accelerated subunit dissociation, slowed subunit addition, and barbed-end uncapping. PubMed: 41931606DOI: 10.1126/sciadv.aee5882 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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