8HFC

Cryo-EM structure of yeast Erf2/Erf4 complex

8HFC の概要

• エントリーDOI: 10.2210/pdb8hfc/pdb
• EMDBエントリー: 34717
• 分子名称: Palmitoyltransferase ERF2, Ras modification protein ERF4, PALMITIC ACID, ... (4 entities in total)
• 機能のキーワード: palmitoyltransferase, saccaromyces cerevisiae, palmitoylation, ras2, transferase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73851.62

構造登録者

Wu, J.,Hu, Q.,Zhang, Y.,Yang, A.,Liu, S. (登録日: 2022-11-10, 公開日: 2023-11-22, 最終更新日: 2025-07-23)

主引用文献

Yang, A.,Liu, S.,Zhang, Y.,Chen, J.,Fan, Y.,Wang, F.,Zou, Y.,Feng, S.,Wu, J.,Hu, Q.
Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation.
Nat.Struct.Mol.Biol., 31:436-446, 2024

PubMed Abstract: Palmitoylation of cysteine residues at the C-terminal hypervariable regions in human HRAS and NRAS, which is necessary for RAS signaling, is catalyzed by the acyltransferase DHHC9 in complex with its accessory protein GCP16. The molecular basis for the acyltransferase activity and the regulation of DHHC9 by GCP16 is not clear. Here we report the cryo-electron microscopy structures of the human DHHC9-GCP16 complex and its yeast counterpart-the Erf2-Erf4 complex, demonstrating that GCP16 and Erf4 are not directly involved in the catalytic process but stabilize the architecture of DHHC9 and Erf2, respectively. We found that a phospholipid binding to an arginine-rich region of DHHC9 and palmitoylation on three residues (C24, C25 and C288) were essential for the catalytic activity of the DHHC9-GCP16 complex. Moreover, we showed that GCP16 also formed complexes with DHHC14 and DHHC18 to catalyze RAS palmitoylation. These findings provide insights into the regulatory mechanism of RAS palmitoyltransferases.

PubMed: 38182928
DOI: 10.1038/s41594-023-01183-5

実験手法

ELECTRON MICROSCOPY (3.5 Å)