8EAS

Yeast VO in complex with Vma12-22p

8EAS の概要

• エントリーDOI: 10.2210/pdb8eas/pdb
• EMDBエントリー: 27984
• 分子名称: Vacuolar ATPase assembly protein VMA22, V-type proton ATPase subunit c, V-type proton ATPase subunit c', ... (11 entities in total)
• 機能のキーワード: v-type, atpase, assembly, proton, membrane 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: 18
• 化学式量合計: 404461.06

構造登録者

Wang, H.,Bueler, S.A.,Rubinstein, J.L. (登録日: 2022-08-29, 公開日: 2022-11-02, 最終更新日: 2025-05-21)

主引用文献

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

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: 36724250
DOI: 10.1073/pnas.2217181120

実験手法

ELECTRON MICROSCOPY (2.6 Å)