6J7F

Complex of GGTaseIII, farnesyl-Ykt6 (C-terminal methylated), and GGPP

6J7F の概要

• エントリーDOI: 10.2210/pdb6j7f/pdb
• 分子名称: Protein prenyltransferase alpha subunit repeat-containing protein 1, Geranylgeranyl transferase type-2 subunit beta, Synaptobrevin homolog YKT6, ... (7 entities in total)
• 機能のキーワード: lipid transferase, lipid binding protein
• 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: 98308.30

構造登録者

Goto-Ito, S.,Yamagata, A.,Sato, Y.,Fukai, S. (登録日: 2019-01-18, 公開日: 2020-01-22, 最終更新日: 2025-05-28)

主引用文献

Shirakawa, R.,Goto-Ito, S.,Goto, K.,Wakayama, S.,Kubo, H.,Sakata, N.,Trinh, D.A.,Yamagata, A.,Sato, Y.,Masumoto, H.,Cheng, J.,Fujimoto, T.,Fukai, S.,Horiuchi, H.
A SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus.
Embo J., 39:e104120-e104120, 2020

PubMed Abstract: Protein prenylation is essential for many cellular processes including signal transduction, cytoskeletal reorganization, and membrane trafficking. Here, we identify a novel type of protein prenyltransferase, which we named geranylgeranyltransferase type-III (GGTase-III). GGTase-III consists of prenyltransferase alpha subunit repeat containing 1 (PTAR1) and the β subunit of RabGGTase. Using a biotinylated geranylgeranyl analogue, we identified the Golgi SNARE protein Ykt6 as a substrate of GGTase-III. GGTase-III transfers a geranylgeranyl group to mono-farnesylated Ykt6, generating doubly prenylated Ykt6. The crystal structure of GGTase-III in complex with Ykt6 provides structural basis for Ykt6 double prenylation. In GGTase-III-deficient cells, Ykt6 remained in a singly prenylated form, and the Golgi SNARE complex assembly was severely impaired. Consequently, the Golgi apparatus was structurally disorganized, and intra-Golgi protein trafficking was delayed. Our findings reveal a fourth type of protein prenyltransferase that generates geranylgeranyl-farnesyl Ykt6. Double prenylation of Ykt6 is essential for the structural and functional organization of the Golgi apparatus.

PubMed: 32128853
DOI: 10.15252/embj.2019104120

実験手法

X-RAY DIFFRACTION (2.883 Å)