6WM2

Human V-ATPase in state 1 with SidK and ADP

6WM2 の概要

• エントリーDOI: 10.2210/pdb6wm2/pdb
• EMDBエントリー: 21847
• 分子名称: V-type proton ATPase subunit E 1, V-type proton ATPase subunit F, V-type proton ATPase 21 kDa proteolipid subunit, ... (29 entities in total)
• 機能のキーワード: v-atpase, proton pump, membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 35
• 化学式量合計: 1275965.31

構造登録者

Wang, L.,Wu, H.,Fu, T.M. (登録日: 2020-04-20, 公開日: 2020-11-11, 最終更新日: 2024-11-20)

主引用文献

Wang, L.,Wu, D.,Robinson, C.V.,Wu, H.,Fu, T.M.
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
Mol.Cell, 80:501-, 2020

PubMed Abstract: Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V complex for ATP hydrolysis and a membrane-embedded V complex for proton transfer. They play important roles in acidification of intracellular vesicles, organelles, and the extracellular milieu in eukaryotes. Here, we report cryoelectron microscopy structures of human V-ATPase in three rotational states at up to 2.9-Å resolution. Aided by mass spectrometry, we build all known protein subunits with associated N-linked glycans and identify glycolipids and phospholipids in the V complex. We define ATP6AP1 as a structural hub for V complex assembly because it connects to multiple V subunits and phospholipids in the c-ring. The glycolipids and the glycosylated V subunits form a luminal glycan coat critical for V-ATPase folding, localization, and stability. This study identifies mechanisms of V-ATPase assembly and biogenesis that rely on the integrated roles of ATP6AP1, glycans, and lipids.

PubMed: 33065002
DOI: 10.1016/j.molcel.2020.09.029

実験手法

ELECTRON MICROSCOPY (3.1 Å)