7ZU0

HOPS tethering complex from yeast

7ZU0 の概要

• エントリーDOI: 10.2210/pdb7zu0/pdb
• EMDBエントリー: 14964 14965 14966 14967 14968 14969 14970
• 分子名称: E3 ubiquitin-protein ligase PEP5, Vacuolar protein sorting-associated protein 16, Vacuolar membrane protein PEP3, ... (6 entities in total)
• 機能のキーワード: hops, tethering complex, lysosome, membrane fusion, rab gtpase, cryo-em, cytosolic protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 636940.21

構造登録者

Shvarev, D.,Schoppe, J.,Koenig, C.,Perz, A.,Fuellbrunn, N.,Kiontke, S.,Langemeyer, L.,Januliene, D.,Schnelle, K.,Kuemmel, D.,Froehlich, F.,Moeller, A.,Ungermann, C. (登録日: 2022-05-11, 公開日: 2022-09-28, 最終更新日: 2025-04-16)

主引用文献

Shvarev, D.,Schoppe, J.,Konig, C.,Perz, A.,Fullbrunn, N.,Kiontke, S.,Langemeyer, L.,Januliene, D.,Schnelle, K.,Kummel, D.,Frohlich, F.,Moeller, A.,Ungermann, C.
Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery.
Elife, 11:-, 2022

PubMed Abstract: Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a conserved heterohexameric tethering complex. On the membranes to be fused, HOPS binds small membrane-associated GTPases and assembles SNAREs for fusion, but how the complex fulfills its function remained speculative. Here, we used cryo-electron microscopy to reveal the structure of HOPS. Unlike previously reported, significant flexibility of HOPS is confined to its extremities, where GTPase binding occurs. The SNARE-binding module is firmly attached to the core, therefore, ideally positioned between the membranes to catalyze fusion. Our data suggest a model for how HOPS fulfills its dual functionality of tethering and fusion and indicate why it is an essential part of the membrane fusion machinery.

PubMed: 36098503
DOI: 10.7554/eLife.80901

実験手法

ELECTRON MICROSCOPY (4.4 Å)