9SGK
F-actin in complex with USP54 M1 actin binding motif
Summary for 9SGK
| Entry DOI | 10.2210/pdb9sgk/pdb |
| EMDB information | 54871 |
| Descriptor | Actin binding motif, Actin, alpha skeletal muscle, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | actin, structural protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 10 |
| Total formula weight | 380454.74 |
| Authors | Yuan, B.,Paraschiakos, T.,Windhorst, S.,Marlovits, T.C. (deposition date: 2025-08-22, release date: 2026-04-29, Last modification date: 2026-07-29) |
| Primary citation | Paraschiakos, T.,Yuan, B.,Hecht-Bucher, M.,Sopelniak, K.,Cervero, P.,Simon, L.,Zonjic, K.,Eggers, D.,Selle, F.,Li, J.,Biabani, A.,Linder, S.,Marlovits, T.C.,Windhorst, S. Evolutionarily conserved short linear motifs drive actin filament binding. Nat.Cell Biol., 28:1437-1452, 2026 Cited by PubMed Abstract: Regulation of the actin cytoskeleton by actin-binding proteins is essential for cellular homeostasis, and the mode of actin binding determines the activity of actin-binding proteins. Here we identify a 'short linear actin filament-binding motif' (SFM) based on the cryo-electron microscopy structure of the ITPKA-actin filament complex. Using the computational pipeline SLiMFold, we discovered 103 human proteins containing SFMs with diverse cellular roles. Phylogenetic analysis suggests that SFMs arose de novo and are conserved across eukaryotes, exhibiting actin filament-binding affinities of 2-12 µM. Critical residues mediating binding and modulating affinity were defined, and the cryo-electron microscopy structures of two SFM-actin filament complexes revealed that SFM binding decreases actin-filament stiffness. These findings indicate that SFMs regulate actin-filament conformation and serve as anchoring modules that connect actin dynamics to a broad variety of cellular functions, providing a framework for understanding the actin-associated roles of numerous proteins. PubMed: 42410114DOI: 10.1038/s41556-026-01979-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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