PDB-6wlw: The Vo region of human V-ATPase in state 1 (focused refinement)

Basic information

• Entry: Database: PDB / ID: 6wlw
• Title: The Vo region of human V-ATPase in state 1 (focused refinement)

Components

• (V-type proton ATPase ...) x 6
• Renin receptor
• Ribonuclease kappa

• Keywords: MEMBRANE PROTEIN / V-ATPase / proton pump

Function / homology

Function:

proton-transporting two-sector ATPase complex / Ion channel transport / intracellular pH reduction / eye pigmentation / central nervous system maturation / transporter activator activity / ATPase-coupled ion transmembrane transporter activity / rostrocaudal neural tube patterning / cellular response to increased oxygen levels / positive regulation of transforming growth factor beta1 production / synaptic vesicle lumen acidification / endosome to plasma membrane protein transport / Golgi lumen acidification / proton-transporting V-type ATPase, V0 domain / Transferrin endocytosis and recycling / plasma membrane proton-transporting V-type ATPase complex / lysosomal lumen acidification / clathrin-coated vesicle membrane / endosomal lumen acidification / vacuolar proton-transporting V-type ATPase, V0 domain / vacuolar transport / XBP1(S) activates chaperone genes / Amino acids regulate mTORC1 / proton-transporting V-type ATPase complex / head morphogenesis / ROS and RNS production in phagocytes / vacuolar proton-transporting V-type ATPase complex / dendritic spine membrane / regulation of cellular pH / vacuolar acidification / osteoclast development / azurophil granule membrane / autophagosome membrane / regulation of MAPK cascade / tertiary granule membrane / ATPase activator activity / ficolin-1-rich granule membrane / positive regulation of Wnt signaling pathway / cilium assembly / RHOA GTPase cycle / transmembrane transporter complex / regulation of macroautophagy / angiotensin maturation / Metabolism of Angiotensinogen to Angiotensins / axon terminus / proton transmembrane transport / Insulin receptor recycling / RNA endonuclease activity / proton-transporting ATPase activity, rotational mechanism / endoplasmic reticulum-Golgi intermediate compartment membrane / proton-transporting ATP synthase activity, rotational mechanism / receptor-mediated endocytosis / secretory granule membrane / transmembrane transport / synaptic vesicle membrane / small GTPase binding / phagocytic vesicle membrane / melanosome / positive regulation of canonical Wnt signaling pathway / signaling receptor activity / ATPase binding / postsynaptic membrane / intracellular iron ion homeostasis / receptor-mediated endocytosis of virus by host cell / Hydrolases; Acting on ester bonds / lysosome / early endosome / endosome membrane / nuclear speck / apical plasma membrane / lysosomal membrane / external side of plasma membrane / axon / Golgi membrane / intracellular membrane-bounded organelle / focal adhesion / ubiquitin protein ligase binding / Neutrophil degranulation / protein-containing complex binding / endoplasmic reticulum membrane / perinuclear region of cytoplasm / Golgi apparatus / extracellular exosome / membrane / plasma membrane / cytosol

Domain/homology:

ATPase, V0 complex, subunit e1/e2, metazoa / V0 complex accessory subunit Ac45 / V-type proton ATPase subunit S1, luminal domain / V-type proton ATPase subunit S1, luminal domain / Renin receptor-like / Renin receptor-like protein / Ribonuclease kappa / V-type proton ATPase subunit S1/VOA1, transmembrane domain / V0 complex accessory subunit Ac45/VOA1 transmembrane domain / ATPase, V0 complex, subunit e1/e2 / ATP synthase subunit H / ATPase, V0 complex, subunit d / V-ATPase proteolipid subunit C, eukaryotic / ATPase, V0 complex, subunit 116kDa, eukaryotic / V-ATPase proteolipid subunit / ATPase, V0 complex, c/d subunit / V-type ATPase subunit C/d / V-type ATP synthase subunit c/d subunit superfamily / V-type ATP synthase c/d subunit, domain 3 superfamily / ATP synthase (C/AC39) subunit / V-type ATPase, V0 complex, 116kDa subunit family / V-type ATPase 116kDa subunit family / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C

Component:

CHOLESTEROL / 1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE / PHOSPHATIDYLETHANOLAMINE / Chem-WJP / Chem-WJS / Chem-WSS / V-type proton ATPase subunit e 1 / Renin receptor / V-type proton ATPase 16 kDa proteolipid subunit c / V-type proton ATPase subunit d 1 / V-type proton ATPase subunit S1 / Ribonuclease kappa / V-type proton ATPase 116 kDa subunit a 1 / V-type proton ATPase 21 kDa proteolipid subunit c''

• Biological species: Homo sapiens (human)
• Method: ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å
• Authors: Wang, L. / Wu, H. / Fu, T.-M.
• Citation: Journal: Mol Cell / Year: 2020; Title: Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.; Authors: Longfei Wang / Di Wu / Carol V Robinson / Hao Wu / Tian-Min Fu / ; 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.

History

Deposition	Apr 20, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Nov 11, 2020	Provider: repository / Type: Initial release
Revision 1.1	Nov 18, 2020	Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.page_first
Revision 1.2	Nov 25, 2020	Group: Data collection / Category: pdbx_entity_branch_descriptor