8EKI

CryoEM structure of the Dsl1 complex bound to SNAREs Sec20 and Use1

8EKI の概要

• エントリーDOI: 10.2210/pdb8eki/pdb
• EMDBエントリー: 28204
• 分子名称: Protein transport protein SEC20, Protein transport protein USE1, Protein transport protein TIP20, ... (5 entities in total)
• 機能のキーワード: tether, snare, complex, transport protein
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 311681.03

構造登録者

DAmico, K.A.,Jeffrey, P.D.,Hughson, F.M. (登録日: 2022-09-21, 公開日: 2023-10-04, 最終更新日: 2024-02-28)

主引用文献

DAmico, K.A.,Stanton, A.E.,Shirkey, J.D.,Travis, S.M.,Jeffrey, P.D.,Hughson, F.M.
Structure of a membrane tethering complex incorporating multiple SNAREs.
Nat.Struct.Mol.Biol., 31:246-254, 2024

PubMed Abstract: Most membrane fusion reactions in eukaryotic cells are mediated by multisubunit tethering complexes (MTCs) and SNARE proteins. MTCs are much larger than SNAREs and are thought to mediate the initial attachment of two membranes. Complementary SNAREs then form membrane-bridging complexes whose assembly draws the membranes together for fusion. Here we present a cryo-electron microscopy structure of the simplest known MTC, the 255-kDa Dsl1 complex of Saccharomyces cerevisiae, bound to the two SNAREs that anchor it to the endoplasmic reticulum. N-terminal domains of the SNAREs form an integral part of the structure, stabilizing a Dsl1 complex configuration with unexpected similarities to the 850-kDa exocyst MTC. The structure of the SNARE-anchored Dsl1 complex and its comparison with exocyst reveal what are likely to be common principles underlying MTC function. Our structure also implies that tethers and SNAREs can work together as a single integrated machine.

PubMed: 38196032
DOI: 10.1038/s41594-023-01164-8

実験手法

ELECTRON MICROSCOPY (4.5 Å)