8RU2
Structure of the F-actin barbed end bound by formin mDia1
Summary for 8RU2
| Entry DOI | 10.2210/pdb8ru2/pdb |
| Related | 8RTT 8RTY 8RU0 |
| EMDB information | 19496 19497 19499 19501 19503 |
| Descriptor | Actin, cytoplasmic 1, N-terminally processed, Methylated-DNA--protein-cysteine methyltransferase,Protein diaphanous homolog 1, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | actin, formin, cdc12, profilin, actin assembly, structural protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 299190.30 |
| Authors | Oosterheert, W.,Boiero Sanders, M.,Funk, J.,Prumbaum, D.,Raunser, S.,Bieling, P. (deposition date: 2024-01-29, release date: 2024-04-10, Last modification date: 2024-04-24) |
| Primary citation | Oosterheert, W.,Boiero Sanders, M.,Funk, J.,Prumbaum, D.,Raunser, S.,Bieling, P. Molecular mechanism of actin filament elongation by formins. Science, 384:eadn9560-eadn9560, 2024 Cited by PubMed Abstract: Formins control the assembly of actin filaments (F-actin) that drive cell morphogenesis and motility in eukaryotes. However, their molecular interaction with F-actin and their mechanism of action remain unclear. In this work, we present high-resolution cryo-electron microscopy structures of F-actin barbed ends bound by three distinct formins, revealing a common asymmetric formin conformation imposed by the filament. Formation of new intersubunit contacts during actin polymerization sterically displaces formin and triggers its translocation. This "undock-and-lock" mechanism explains how actin-filament growth is coordinated with formin movement. Filament elongation speeds are controlled by the positioning and stability of actin-formin interfaces, which distinguish fast and slow formins. Furthermore, we provide a structure of the actin-formin-profilin ring complex, which resolves how profilin is rapidly released from the barbed end during filament elongation. PubMed: 38603491DOI: 10.1126/science.adn9560 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.49 Å) |
Structure validation
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