8DNH

Cryo-EM structure of nonmuscle beta-actin

8DNH の概要

• エントリーDOI: 10.2210/pdb8dnh/pdb
• EMDBエントリー: 27572
• 分子名称: Actin, cytoplasmic 1, N-terminally processed, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: cytoskeleton, structural protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 168568.10

構造登録者

Arora, A.S.,Huang, H.L.,Heissler, S.M.,Chinthalapudi, K. (登録日: 2022-07-11, 公開日: 2023-04-12)

主引用文献

Arora, 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

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

実験手法

ELECTRON MICROSCOPY (2.99 Å)