6WM2
Human V-ATPase in state 1 with SidK and ADP
Summary for 6WM2
Entry DOI | 10.2210/pdb6wm2/pdb |
EMDB information | 21847 |
Descriptor | 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) |
Functional Keywords | v-atpase, proton pump, membrane protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 35 |
Total formula weight | 1275965.31 |
Authors | |
Primary citation | 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 Cited by 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: 33065002DOI: 10.1016/j.molcel.2020.09.029 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
Download full validation report