7ahq
From Proteopedia
Cryo-EM structure of F-actin stabilized by trans-optoJASP-8
Structural highlights
Publication Abstract from PubMedActin 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. Cryo-EM resolves molecular recognition of an optojasp photoswitch bound to actin filaments in both switch states.,Pospich S, Kullmer F, Nasufovic V, Funk J, Belyy A, Bieling P, Arndt HD, Raunser S Angew Chem Int Ed Engl. 2021 Jan 15. doi: 10.1002/anie.202013193. PMID:33449370[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||
