7ZU0
HOPS tethering complex from yeast
Summary for 7ZU0
| Entry DOI | 10.2210/pdb7zu0/pdb |
| EMDB information | 14964 14965 14966 14967 14968 14969 14970 |
| Descriptor | E3 ubiquitin-protein ligase PEP5, Vacuolar protein sorting-associated protein 16, Vacuolar membrane protein PEP3, ... (6 entities in total) |
| Functional Keywords | hops, tethering complex, lysosome, membrane fusion, rab gtpase, cryo-em, cytosolic protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 6 |
| Total formula weight | 636940.21 |
| Authors | 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. (deposition date: 2022-05-11, release date: 2022-09-28, Last modification date: 2024-07-24) |
| Primary citation | Shvarev, D.,Konig, C.,Susan, N.,Langemeyer, L.,Walter, S.,Perz, A.,Frohlich, F.,Ungermann, C.,Moeller, A. Structure of the endosomal CORVET tethering complex. Nat Commun, 15:5227-5227, 2024 Cited by PubMed Abstract: Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by the Rab5 GTPase and its effector, the hexameric CORVET tethering complex, which is homologous to the lysosomal HOPS. How these related complexes recognize their specific target membranes remains entirely elusive. Here, we solve the structure of CORVET by cryo-electron microscopy and revealed its minimal requirements for membrane tethering. As expected, the core of CORVET and HOPS resembles each other. However, the function-defining subunits show marked structural differences. Notably, we discover that unlike HOPS, CORVET depends not only on Rab5 but also on phosphatidylinositol-3-phosphate (PI3P) and membrane lipid packing defects for tethering, implying that an organelle-specific membrane code enables fusion. Our data suggest that both shape and membrane interactions of CORVET and HOPS are conserved in metazoans, thus providing a paradigm how tethering complexes function. PubMed: 38898033DOI: 10.1038/s41467-024-49137-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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