6VQG

Mammalian V-ATPase from rat brain membrane-embedded Vo region rotational state 2 (from focused refinement)

Summary for 6VQG

• Entry DOI: 10.2210/pdb6vqg/pdb
• EMDB information: 21349
• Descriptor: ATPase H+-transporting V1 subunit D, Renin receptor, V-type proton ATPase subunit F, ... (10 entities in total)
• Functional Keywords: membrane protein complex, rotary atpase, proton transport
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 18
• Total formula weight: 452962.67

Authors

Abbas, Y.M.,Rubinstein, J.L. (deposition date: 2020-02-05, release date: 2020-03-18, Last modification date: 2024-03-06)

Primary citation

Abbas, Y.M.,Wu, D.,Bueler, S.A.,Robinson, C.V.,Rubinstein, J.L.
Structure of V-ATPase from the mammalian brain.
Science, 367:1240-1246, 2020

PubMed Abstract: In neurons, the loading of neurotransmitters into synaptic vesicles uses energy from proton-pumping vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases). These membrane protein complexes possess numerous subunit isoforms, which complicates their analysis. We isolated homogeneous rat brain V-ATPase through its interaction with SidK, a effector protein. Cryo-electron microscopy allowed the construction of an atomic model, defining the enzyme's ATP:proton ratio as 3:10 and revealing a homolog of yeast subunit f in the membrane region, which we tentatively identify as RNAseK. The c ring encloses the transmembrane anchors for cleaved ATP6AP1/Ac45 and ATP6AP2/PRR, the latter of which is the (pro)renin receptor that, in other contexts, is involved in both Wnt signaling and the renin-angiotensin system that regulates blood pressure. This structure shows how ATP6AP1/Ac45 and ATP6AP2/PRR enable assembly of the enzyme's catalytic and membrane regions.

PubMed: 32165585
DOI: 10.1126/science.aaz2924

Experimental method

ELECTRON MICROSCOPY (4.2 Å)