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Title | Cryo-EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States. |
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Journal, issue, pages | Angew Chem Int Ed Engl, Vol. 60, Issue 16, Page 8678-8682, Year 2021 |
Publish date | Apr 12, 2021 |
Authors | Sabrina Pospich / Florian Küllmer / Veselin Nasufović / Johanna Funk / Alexander Belyy / Peter Bieling / Hans-Dieter Arndt / Stefan Raunser / |
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 ...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. |
External links | Angew Chem Int Ed Engl / PubMed:33449370 / PubMed Central |
Methods | EM (helical sym.) / EM (single particle) |
Resolution | 2.9 - 3.6 Å |
Structure data | EMDB-11787, PDB-7ahn: EMDB-11790, PDB-7ahq: |
Chemicals | ChemComp-ADP: ChemComp-MG: ChemComp-PO4: ChemComp-RLZ: |
Source |
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Keywords | STRUCTURAL PROTEIN / Cytoskeleton / jasplakinolide / azobenzene photoswitch / stabilized-actin filament |