8f8t

Cryo-EM structure of the Tropomodulin-capped pointed end of F-actin

spinqualitylabelsall models 8f8t, resolution 3.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8f8t is a 8 chain structure with sequence from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.26Å Ligands: ADP, HIC, MG 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 The barbed and pointed ends of the actin filament (F-actin) are the sites of growth/shrinkage and the targets of capping proteins that block subunit exchange, including CapZ at the barbed end and tropomodulin at the pointed end. We describe cryo-electron microscopy structures of the free and capped ends of F-actin. Terminal subunits at the free barbed end adopt a "flat" F-actin conformation. CapZ binds with minor changes to the barbed end but major changes to itself. In contrast, subunits at the free pointed end adopt a "twisted" G-actin conformation. Tropomodulin binding forces the second subunit into an F-actin conformation. The structures reveal how the ends differ from the middle in F-actin and how these differences control subunit addition/dissociation, capping, and interactions with end-binding proteins. Structures of the free and capped ends of the actin filament.,Carman PJ, Barrie KR, Rebowski G, Dominguez R Science. 2023 May 25:eadg6812. doi: 10.1126/science.adg6812. PMID:37228182 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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