7CZB

The cryo-EM structure of the ERAD retrotranslocation channel formed by human Derlin-1

7CZB の概要

• エントリーDOI: 10.2210/pdb7czb/pdb
• EMDBエントリー: 30508
• 分子名称: Derlin-1 (1 entity in total)
• 機能のキーワード: endoplasmic reticulum associated degradation, retrotranslocation, cryo-em, transmembrane channels, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 115286.66

構造登録者

Rao, B.,Li, S.,Yao, D.,Wang, Q.,Xia, Y.,Jia, Y.,Shen, Y.,Cao, Y. (登録日: 2020-09-07, 公開日: 2021-03-17, 最終更新日: 2024-03-27)

主引用文献

Rao, B.,Li, S.,Yao, D.,Wang, Q.,Xia, Y.,Jia, Y.,Shen, Y.,Cao, Y.
The cryo-EM structure of an ERAD protein channel formed by tetrameric human Derlin-1.
Sci Adv, 7:-, 2021

PubMed Abstract: Endoplasmic reticulum-associated degradation (ERAD) is a process directing misfolded proteins from the ER lumen and membrane to the degradation machinery in the cytosol. A key step in ERAD is the translocation of ER proteins to the cytosol. Derlins are essential for protein translocation in ERAD, but the mechanism remains unclear. Here, we solved the structure of human Derlin-1 by cryo-electron microscopy. The structure shows that Derlin-1 forms a homotetramer that encircles a large tunnel traversing the ER membrane. The tunnel has a diameter of about 12 to 15 angstroms, large enough to allow an α helix to pass through. The structure also shows a lateral gate within the membrane, providing access of transmembrane proteins to the tunnel, and thus, human Derlin-1 forms a protein channel for translocation of misfolded proteins. Our structure is different from the monomeric yeast Derlin structure previously reported, which forms a semichannel with another protein.

PubMed: 33658201
DOI: 10.1126/sciadv.abe8591

実験手法

ELECTRON MICROSCOPY (3.8 Å)