3JBJ

Cryo-EM reconstruction of F-actin

Summary for 3JBJ

• Entry DOI: 10.2210/pdb3jbj/pdb
• Related: 3JBI 3JBK
• EMDB information: 6446 6447 6448 6449 6450 6451
• Descriptor: Actin, alpha skeletal muscle, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: actin, cell migration, adhesion, mechanosensation, cytoskeleton, structural protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Total number of polymer chains: 2
• Total formula weight: 84628.24

Authors

Kim, L.Y.,Thompson, P.M.,Lee, H.T.,Pershad, M.,Campbell, S.L.,Alushin, G.M. (deposition date: 2015-09-03, release date: 2015-11-04, Last modification date: 2024-02-21)

Primary citation

Kim, L.Y.,Thompson, P.M.,Lee, H.T.,Pershad, M.,Campbell, S.L.,Alushin, G.M.
The Structural Basis of Actin Organization by Vinculin and Metavinculin.
J.Mol.Biol., 428:10-25, 2016

PubMed Abstract: 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-Å-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.

PubMed: 26493222
DOI: 10.1016/j.jmb.2015.09.031

Experimental method

ELECTRON MICROSCOPY (7.6 Å)