8F8Q

Cryo-EM structure of the CapZ-capped barbed end of F-actin

8F8Q の概要

• エントリーDOI: 10.2210/pdb8f8q/pdb
• EMDBエントリー: 28932 28933 28934 28935 28936
• 分子名称: Actin, alpha skeletal muscle, F-actin-capping protein subunit alpha-1, F-actin-capping protein subunit beta, ... (5 entities in total)
• 機能のキーワード: barbed end capping protein, f-actin, capz, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 319591.89

構造登録者

Carman, P.J.,Barrie, K.R.,Dominguez, R. (登録日: 2022-11-22, 公開日: 2023-06-07, 最終更新日: 2023-07-05)

主引用文献

Carman, P.J.,Barrie, K.R.,Rebowski, G.,Dominguez, R.
Structures of the free and capped ends of the actin filament.
Science, 380:1287-1292, 2023

PubMed Abstract: The barbed and pointed ends of the actin filament (F-actin) are the sites of growth and shrinkage and the targets of capping proteins that block subunit exchange, including CapZ at the barbed end and tropomodulin at the pointed end. We describe cryo-electron microscopy structures of the free and capped ends of F-actin. Terminal subunits at the free barbed end adopt a "flat" F-actin conformation. CapZ binds with minor changes to the barbed end but with major changes to itself. By contrast, subunits at the free pointed end adopt a "twisted" monomeric actin (G-actin) conformation. Tropomodulin binding forces the second subunit into an F-actin conformation. The structures reveal how the ends differ from the middle in F-actin and how these differences control subunit addition, dissociation, capping, and interactions with end-binding proteins.

PubMed: 37228182
DOI: 10.1126/science.adg6812

実験手法

ELECTRON MICROSCOPY (2.79 Å)