7AHQ
Cryo-EM structure of F-actin stabilized by trans-optoJASP-8
Summary for 7AHQ
| Entry DOI | 10.2210/pdb7ahq/pdb |
| Related | 7AHN |
| EMDB information | 11787 11790 |
| Descriptor | Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | cytoskeleton, jasplakinolide, azobenzene photoswitch, stabilized-actin filament, structural protein |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 5 |
| Total formula weight | 218648.45 |
| Authors | Pospich, S.,Raunser, S. (deposition date: 2020-09-25, release date: 2021-01-27, Last modification date: 2025-04-09) |
| Primary citation | Pospich, S.,Kullmer, F.,Nasufovic, V.,Funk, J.,Belyy, A.,Bieling, P.,Arndt, H.D.,Raunser, S. Cryo-EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States. Angew.Chem.Int.Ed.Engl., 60:8678-8682, 2021 Cited by PubMed Abstract: Actin is essential for key processes in all eukaryotic cells. Cellpermeable optojasps provide spatiotemporal control of the actin cytoskeleton, confining toxicity and potentially rendering F-actin druggable by photopharmacology. Here, we report cryo electron microscopy (cryo-EM) structures of both isomeric states of one optojasp bound to actin filaments. The high-resolution structures reveal for the first time the pronounced effects of photoswitching a functionalized azobenzene. By characterizing the optojasp binding site and identifying conformational changes within F-actin that depend on the optojasp isomeric state, we refine determinants for the design of functional F-actin photoswitches. PubMed: 33449370DOI: 10.1002/anie.202013193 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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