8EAT
Yeast VO missing subunits a, e, and f in complex with Vma12-22p
Summary for 8EAT
Entry DOI | 10.2210/pdb8eat/pdb |
EMDB information | 27985 |
Descriptor | Vacuolar ATPase assembly protein VMA22, Vacuolar ATPase assembly integral membrane protein VPH2, V-type proton ATPase subunit F, ... (8 entities in total) |
Functional Keywords | v-type proton atpase, membrane protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 15 |
Total formula weight | 299943.91 |
Authors | Wang, H.,Bueler, S.A.,Rubinstein, J.L. (deposition date: 2022-08-29, release date: 2022-11-02, Last modification date: 2025-05-14) |
Primary citation | Wang, H.,Bueler, S.A.,Rubinstein, J.L. Structural basis of V-ATPase V O region assembly by Vma12p, 21p, and 22p. Proc.Natl.Acad.Sci.USA, 120:e2217181120-e2217181120, 2023 Cited by PubMed Abstract: Vacuolar-type adenosine triphosphatases (V-ATPases) are rotary proton pumps that acidify specific intracellular compartments in almost all eukaryotic cells. These multi-subunit enzymes consist of a soluble catalytic V region and a membrane-embedded proton-translocating V region. V is assembled in the endoplasmic reticulum (ER) membrane, and V is assembled in the cytosol. However, V binds V only after V is transported to the Golgi membrane, thereby preventing acidification of the ER. We isolated V complexes and subcomplexes from bound to V-ATPase assembly factors Vma12p, Vma21p, and Vma22p. Electron cryomicroscopy shows how the Vma12-22p complex recruits subunits a, e, and f to the rotor ring of V while blocking premature binding of V. Vma21p, which contains an ER-retrieval motif, binds the V:Vma12-22p complex, "mature" V, and a complex that appears to contain a ring of loosely packed rotor subunits and the proteins YAR027W and YAR028W. The structures suggest that Vma21p binds assembly intermediates that contain a rotor ring and that activation of proton pumping following assembly of V with V removes Vma21p, allowing V-ATPase to remain in the Golgi. Together, these structures show how Vma12-22p and Vma21p function in V-ATPase assembly and quality control, ensuring the enzyme acidifies only its intended cellular targets. PubMed: 36724250DOI: 10.1073/pnas.2217181120 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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