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8DMY

Cryo-EM structure of cardiac muscle alpha-actin

Summary for 8DMY
Entry DOI10.2210/pdb8dmy/pdb
EMDB information27549
DescriptorActin, alpha cardiac muscle 1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordscytoskeleton, structural protein
Biological sourceBos taurus (domestic cattle)
Total number of polymer chains4
Total formula weight168719.94
Authors
Arora, A.S.,Huang, H.L.,Heissler, S.M.,Chinthalapudi, K. (deposition date: 2022-07-09, release date: 2023-04-12, Last modification date: 2026-08-05)
Primary citationArora, A.S.,Huang, H.L.,Singh, R.,Narui, Y.,Suchenko, A.,Hatano, T.,Heissler, S.M.,Balasubramanian, M.K.,Chinthalapudi, K.
Structural insights into actin isoforms.
Elife, 12:-, 2023
Cited by
PubMed Abstract: Actin isoforms organize into distinct networks that are essential for the normal function of eukaryotic cells. Despite a high level of sequence and structure conservation, subtle differences in their design principles determine the interaction with myosin motors and actin-binding proteins. Therefore, identifying how the structure of actin isoforms relates to function is important for our understanding of normal cytoskeletal physiology. Here, we report the high-resolution structures of filamentous skeletal muscle α-actin (3.37 Å), cardiac muscle α-actin (3.07 Å), ß-actin (2.99 Å), and γ-actin (3.38 Å) in the Mg·ADP state with their native post-translational modifications. The structures revealed isoform-specific conformations of the N-terminus that shift closer to the filament surface upon myosin binding, thereby establishing isoform-specific interfaces. Collectively, the structures of single-isotype, post-translationally modified bare skeletal muscle α-actin, cardiac muscle α-actin, ß-actin, and γ-actin reveal general principles, similarities, and differences between isoforms. They complement the repertoire of known actin structures and allow for a comprehensive understanding of in vitro and in vivo functions of actin isoforms.
PubMed: 36790143
DOI: 10.7554/eLife.82015
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.07 Å)
Structure validation

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