6ZZZ

Crystal structure of yeast Sec62 cytoplasmic domain

6ZZZ の概要

• エントリーDOI: 10.2210/pdb6zzz/pdb
• 分子名称: Translocation protein SEC62, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: sec62, sec62 domain, post translocon, protein transport
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32160.91

構造登録者

Cheng, J.,Beckmann, R. (登録日: 2020-08-05, 公開日: 2020-12-02, 最終更新日: 2024-10-16)

主引用文献

Weng, T.H.,Steinchen, W.,Beatrix, B.,Berninghausen, O.,Becker, T.,Bange, G.,Cheng, J.,Beckmann, R.
Architecture of the active post-translational Sec translocon.
Embo J., 40:e105643-e105643, 2021

PubMed Abstract: In eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel (PCC). In the post-translational mode, fully synthesized proteins are recognized by a specialized channel additionally containing the Sec62, Sec63, Sec71, and Sec72 subunits. Recent structures of this Sec complex in the idle state revealed the overall architecture in a pre-opened state. Here, we present a cryo-EM structure of the yeast Sec complex bound to a substrate, and a crystal structure of the Sec62 cytosolic domain. The signal sequence is inserted into the lateral gate of Sec61α similar to previous structures, yet, with the gate adopting an even more open conformation. The signal sequence is flanked by two Sec62 transmembrane helices, the cytoplasmic N-terminal domain of Sec62 is more rigidly positioned, and the plug domain is relocated. We crystallized the Sec62 domain and mapped its interaction with the C-terminus of Sec63. Together, we obtained a near-complete and integrated model of the active Sec complex.

PubMed: 33305433
DOI: 10.15252/embj.2020105643

実験手法

X-RAY DIFFRACTION (2.54 Å)