6wm2

Human V-ATPase in state 1 with SidK and ADP

spinqualitylabelsall models 6wm2, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6wm2 is a 12 chain structure with sequence from Homo sapiens and Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: ADP, BGC, BMA, CLR, GAL, GLC, MAN, NAG, NGA, PSF, PTY, SIA, WJP, WJS, WSS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VATD_HUMAN Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (PubMed:21844891).[UniProtKB:P39942] Publication Abstract from PubMed Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V1 complex for ATP hydrolysis and a membrane-embedded Vo 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-A resolution. Aided by mass spectrometry, we build all known protein subunits with associated N-linked glycans and identify glycolipids and phospholipids in the Vo complex. We define ATP6AP1 as a structural hub for Vo complex assembly because it connects to multiple Vo subunits and phospholipids in the c-ring. The glycolipids and the glycosylated Vo 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. Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.,Wang L, Wu D, Robinson CV, Wu H, Fu TM Mol Cell. 2020 Nov 5;80(3):501-511.e3. doi: 10.1016/j.molcel.2020.09.029. Epub, 2020 Oct 15. PMID:33065002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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