+検索条件
-Structure paper
タイトル | Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly. |
---|---|
ジャーナル・号・ページ | Mol Cell, Vol. 80, Issue 3, Page 501-511.e3, Year 2020 |
掲載日 | 2020年11月5日 |
![]() | Longfei Wang / Di Wu / Carol V Robinson / Hao Wu / Tian-Min Fu / ![]() ![]() |
PubMed 要旨 | 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 ...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. |
![]() | ![]() ![]() ![]() |
手法 | EM (単粒子) |
解像度 | 2.9 - 3.6 Å |
構造データ | EMDB-21844, PDB-6wlw: EMDB-21845, PDB-6wlz: EMDB-21847, PDB-6wm2: EMDB-21848, PDB-6wm3: EMDB-21849, PDB-6wm4: |
化合物 | ![]() ChemComp-WSS: ![]() ChemComp-PTY: ![]() ChemComp-WJS: ![]() ChemComp-CLR: ![]() ChemComp-PSF: ![]() ChemComp-WJP: ![]() ChemComp-NAG: ![]() ChemComp-ADP: |
由来 |
|
![]() | MEMBRANE PROTEIN / V-ATPase / proton pump / pump |