6NAS

Ternary Complex of Ac-Alpha-Actin with Profilin and AcCoA-NAA80

6NAS の概要

• エントリーDOI: 10.2210/pdb6nas/pdb
• 分子名称: Actin, alpha skeletal muscle, N-alpha-acetyltransferase 80, Profilin-1, ... (10 entities in total)
• 機能のキーワード: acetylation, naa80, cytosolic protein, structural protein-transferase complex, structural protein/transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 85135.83

構造登録者

Rebowski, G.,Boczkowska, M.,Dominguez, R. (登録日: 2018-12-06, 公開日: 2020-01-29, 最終更新日: 2023-10-11)

主引用文献

Rebowski, G.,Boczkowska, M.,Drazic, A.,Ree, R.,Goris, M.,Arnesen, T.,Dominguez, R.
Mechanism of actin N-terminal acetylation.
Sci Adv, 6:eaay8793-eaay8793, 2020

PubMed Abstract: About 80% of human proteins are amino-terminally acetylated (Nt-acetylated) by one of seven Nt-acetyltransferases (NATs). Actin, the most abundant protein in the cytoplasm, has its own dedicated NAT, NAA80, which acts posttranslationally and affects cytoskeleton assembly and cell motility. Here, we show that NAA80 does not associate with filamentous actin in cells, and its natural substrate is the monomeric actin-profilin complex, consistent with Nt-acetylation preceding polymerization. NAA80 Nt-acetylates actin-profilin much more efficiently than actin alone, suggesting that profilin acts as a chaperone for actin Nt-acetylation. We determined crystal structures of the NAA80-actin-profilin ternary complex, representing different actin isoforms and different states of the catalytic reaction and revealing the first structure of NAT-substrate complex at atomic resolution. The structural, biochemical, and cellular analysis of mutants shows how NAA80 has evolved to specifically recognize actin among all cellular proteins while targeting all six actin isoforms, which differ the most at the amino terminus.

PubMed: 32284999
DOI: 10.1126/sciadv.aay8793

実験手法

X-RAY DIFFRACTION (2.9 Å)