7ZTY

Structure of Vps39 N-terminal domain from Chaetomium thermophilum

Summary for 7ZTY

• Entry DOI: 10.2210/pdb7zty/pdb
• Descriptor: CNH domain-containing protein (2 entities in total)
• Functional Keywords: tethering, membrane fusion, gtpase effector, hops, transport protein
• Biological source: Chaetomium thermophilum
• Total number of polymer chains: 1
• Total formula weight: 54944.36

Authors

Kiontke, S.,Ungermann, C.,Kuemmel, D. (deposition date: 2022-05-11, release date: 2022-09-21, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.89 Å)