7ahq | pdb_00007ahq

Cryo-EM structure of F-actin stabilized by trans-optoJASP-8

spinqualitylabelsall models 7ahq, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ahq is a 5 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG, PO4, RLZ NonStd Res: HIC Related: 7ahn Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin 3D structures

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