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Our muscle at near-atomic resolution – Cryo-EM structure of the F-actin-tropomyosin complex.

Abstract number: 8368

Session Code: LS01-S04

DOI: 10.1002/9783527808465.EMC2016.8368

Meeting: The 16th European Microscopy Congress 2016

Session: Life Sciences

Topic: Macromolecular assemblies, supra molecular assemblies

Presentation Form: Invited Speaker

Corresponding Email: julian.von-der-ecken@mpi-dortmund.mpg.de

Julian von der Ecken (1), Mirco Müller (2), William Lehman (3), Dietmar J. Manstein (2), Pawel A. Penczek (4), Stefan Raunser (1)

1. Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Allemagne 2. Institute for Biophysical Chemistry, Hannover Medical School, Hannover, Allemagne 3. Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Etats-Unis 4. Department of Biochemistry and Molecular Biology, Houston Medical School, Houston, Etats-Unis

Keywords: cryo-EM, cytoskeleton, F-actin, filament, polymer, structure, tropomyosin

Muscular movement plays an essential role not only in our lives but also describes a fundamental mechanism of force production. Filamentous actin (F-actin) is the major protein of muscle thin filaments, and actin microfilaments are the main component of the eukaryotic cytoskeleton. The interaction of myosin with actin filaments is the central feature of muscle contraction and cargo movement along actin filaments. In striated muscle fibres, this interplay is mainly regulated by tropomyosin and troponin. Although crystal structures for monomeric actin are available, the difficulty of obtaining diffracting crystals, however, has prevented structure determination by crystallography of F-actin. High-resolution structures of F-actin in complex are still missing, hampering our understanding of how disease-causing mutations affect the function of thin muscle filaments and affecting skeletal and cardiac muscles.

We solved the three-dimensional structure of F-actin in complex with tropomyosin at a resolution of 3.7 Å (von der Ecken et al., 2015). We used cutting edge transmission electron cryomicroscopy and direct electron detectors and implemented new methods for processing of the data. The structure reveals insights in the inner interaction of the F-actin subunits and the interplay of F-actin and tropomyosin at near-atomic resolution.

Reference:

von der Ecken J., Müller M., Lehman W., Manstein D.J., Penczek P.A., Raunser S. (2015): Structure of the F-actin-tropomyosin complex. Nature 519, 114-117.

Figures:

Cryo-EM stucture of skeletal F-actin-tropomyosin complex at near-atomic resolution.

To cite this abstract:

Julian von der Ecken, Mirco Müller, William Lehman, Dietmar J. Manstein, Pawel A. Penczek, Stefan Raunser; Our muscle at near-atomic resolution – Cryo-EM structure of the F-actin-tropomyosin complex.. The 16th European Microscopy Congress, Lyon, France. https://emc-proceedings.com/abstract/our-muscle-at-near-atomic-resolution-cryo-em-structure-of-the-f-actin-tropomyosin-complex/. Accessed: December 2, 2023
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