4Z79

Leiomodin-1 Actin-Binding Site 2 (ABS2)

4Z79 の概要

• エントリーDOI: 10.2210/pdb4z79/pdb
• 関連するPDBエントリー: 4Z8G 4Z94
• 分子名称: Leiomodin-1 Actin-Binding Site 2 (ABS2), GLYCEROL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: leiomodin-1 actin binding site 2 abs2 actin nucleator, protein binding
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21925.30

構造登録者

Rebowski, G.,Boczkowska, M.,Dominguez, R. (登録日: 2015-04-06, 公開日: 2015-10-21, 最終更新日: 2023-09-27)

主引用文献

Boczkowska, M.,Rebowski, G.,Kremneva, E.,Lappalainen, P.,Dominguez, R.
How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.
Nat Commun, 6:8314-8314, 2015

PubMed Abstract: How proteins sharing a common fold have evolved different functions is a fundamental question in biology. Tropomodulins (Tmods) are prototypical actin filament pointed-end-capping proteins, whereas their homologues, Leiomodins (Lmods), are powerful filament nucleators. We show that Tmods and Lmods do not compete biochemically, and display similar but distinct localization in sarcomeres. Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt their functions for capping versus nucleation. Tmods have alternating tropomyosin (TM)- and actin-binding sites (TMBS1, ABS1, TMBS2 and ABS2). Lmods additionally contain a C-terminal extension featuring an actin-binding WH2 domain. Unexpectedly, the different activities of Tmods and Lmods do not arise from the Lmod-specific extension. Instead, nucleation by Lmods depends on two major adaptations-the loss of pointed-end-capping elements present in Tmods and the specialization of the highly conserved ABS2 for recruitment of two or more actin subunits. The WH2 domain plays only an auxiliary role in nucleation.

PubMed: 26370058
DOI: 10.1038/ncomms9314

実験手法

X-RAY DIFFRACTION (1.54 Å)