3jbj | pdb_00003jbj

Cryo-EM reconstruction of F-actin

spinqualitylabelsall models 3jbj, resolution 7.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jbj is a 2 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 Related: 3jbi, 3jbk Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 Vinculin is an essential adhesion protein that links membrane-bound integrin and cadherin receptors through their intracellular binding partners to filamentous actin, facilitating mechanotransduction. Here we present an 8.5-A-resolution cryo-electron microscopy reconstruction and pseudo-atomic model of the vinculin tail (Vt) domain bound to F-actin. Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the Vt helical bundle to mediate actin bundling. We find that an analogous conformational change also occurs in the H1' helix of the tail domain of metavinculin (MVt) upon actin binding, a muscle-specific splice isoform that suppresses actin bundling by Vt. These data support a model in which metavinculin tunes the actin bundling activity of vinculin in a tissue-specific manner, providing a mechanistic framework for understanding metavinculin mutations associated with hereditary cardiomyopathies. The Structural Basis of Actin Organization by Vinculin and Metavinculin.,Kim LY, Thompson PM, Lee HT, Pershad M, Campbell SL, Alushin GM J Mol Biol. 2016 Jan 16;428(1):10-25. doi: 10.1016/j.jmb.2015.09.031. Epub 2015, Oct 20. PMID:26493222 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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