9HM9

Structure of the optimized F-tractin in complex with F-actin

9HM9 の概要

• エントリーDOI: 10.2210/pdb9hm9/pdb
• 関連するPDBエントリー: 9GOB
• EMDBエントリー: 52289
• 分子名称: Actin, alpha skeletal muscle, Inositol-trisphosphate 3-kinase A, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: actin, f-tractin, cytosolic protein
• 由来する生物種: Oryctolagus cuniculus (rabbit); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 213305.83

構造登録者

Shatskiy, D.,Belyy, A. (登録日: 2024-12-07, 公開日: 2025-01-22, 最終更新日: 2025-07-09)

主引用文献

Shatskiy, D.,Sivan, A.,Wedlich-Soldner, R.,Belyy, A.
Structure of the F-tractin-F-actin complex.
J.Cell Biol., 224:-, 2025

PubMed Abstract: F-tractin is a peptide widely used to visualize the actin cytoskeleton in live eukaryotic cells but has been reported to impair cell migration and induce actin bundling at high expression levels. To elucidate these effects, we determined the cryo-EM structure of the F-tractin-F-actin complex, revealing that F-tractin consists of a flexible N-terminal region and an amphipathic C-terminal helix. The N-terminal part is dispensable for F-actin binding but responsible for the bundling effect. Based on these insights, we developed an optimized F-tractin, which eliminates the N-terminal region and minimizes bundling while retaining strong actin labeling. The C-terminal helix interacts with a hydrophobic pocket formed by two neighboring actin subunits, an interaction region shared by many actin-binding polypeptides, including the popular actin-binding probe Lifeact. Thus, rather than contrasting F-tractin and Lifeact, our data indicate that these peptides have analogous modes of interaction with F-actin. Our study dissects the structural elements of F-tractin and provides a foundation for developing future actin probes.

PubMed: 39928047
DOI: 10.1083/jcb.202409192

実験手法

ELECTRON MICROSCOPY (3.4 Å)