Structural highlights
Function
[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Publication Abstract from PubMed
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.
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 Also
References
- ↑ Pospich S, Kullmer F, Nasufovic V, Funk J, Belyy A, Bieling P, Arndt HD, Raunser S. Cryo-EM resolves molecular recognition of an optojasp photoswitch bound to actin filaments in both switch states. Angew Chem Int Ed Engl. 2021 Jan 15. doi: 10.1002/anie.202013193. PMID:33449370 doi:http://dx.doi.org/10.1002/anie.202013193
