4UUY

Structural Identification of the Vps18 beta-propeller reveals a critical role in the HOPS complex stability and function.

Summary for 4UUY

• Entry DOI: 10.2210/pdb4uuy/pdb
• Descriptor: VACUOLAR MEMBRANE PROTEIN PEP3, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: transport protein, hops, membrane fusion, vacuole, endosome
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Vacuole membrane; Peripheral membrane protein; Cytoplasmic side: P27801
• Total number of polymer chains: 2
• Total formula weight: 81757.36

Authors

Behrmann, H.,Gohlke, U.,Heinemann, U. (deposition date: 2014-08-01, release date: 2014-10-29, Last modification date: 2024-05-08)

Primary citation

Behrmann, H.,Lurick, A.,Kuhlee, A.,Balderhaar, H.K.,Brocker, C.,Kummel, D.,Engelbrecht-Vandre, S.,Gohlke, U.,Raunser, S.,Heinemann, U.,Ungermann, C.
Structural Identification of the Vps18 Beta-Propeller Reveals a Critical Role in the Hops Complex Stability and Function.
J.Biol.Chem., 289:33503-, 2014

PubMed Abstract: Membrane fusion at the vacuole, the lysosome equivalent in yeast, requires the HOPS tethering complex, which is recruited by the Rab7 GTPase Ypt7. HOPS provides a template for the assembly of SNAREs and thus likely confers fusion at a distinct position on vacuoles. Five of the six subunits in HOPS have a similar domain prediction with strong similarity to COPII subunits and nuclear porins. Here, we show that Vps18 indeed has a seven-bladed β-propeller as its N-terminal domain by revealing its structure at 2.14 Å. The Vps18 N-terminal domain can interact with the N-terminal part of Vps11 and also binds to lipids. Although deletion of the Vps18 N-terminal domain does not preclude HOPS assembly, as revealed by negative stain electron microscopy, the complex is instable and cannot support membrane fusion in vitro. We thus conclude that the β-propeller of Vps18 is required for HOPS stability and function and that it can serve as a starting point for further structural analyses of the HOPS tethering complex.

PubMed: 25324549
DOI: 10.1074/JBC.M114.602714

Experimental method

X-RAY DIFFRACTION (2.14 Å)