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-Structure paper
タイトル | Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly. |
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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 |
著者 | 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. |
リンク | Mol Cell / PubMed:33065002 / PubMed Central |
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 |
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キーワード | MEMBRANE PROTEIN / V-ATPase / proton pump / pump |