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Cryo‐EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States
Author(s) -
Pospich Sabrina,
Küllmer Florian,
Nasufović Veselin,
Funk Johanna,
Belyy Alexander,
Bieling Peter,
Arndt HansDieter,
Raunser Stefan
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202013193
Subject(s) - photoswitch , actin , cytoskeleton , biophysics , chemistry , actin binding protein , actin cytoskeleton , treadmilling , biology , microfilament , cell , biochemistry , photochemistry
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.