6VQC
Mammalian V-ATPase from rat brain membrane-embedded Vo region rotational state 1 (from focused refinement)
Summary for 6VQC
| Entry DOI | 10.2210/pdb6vqc/pdb |
| EMDB information | 21348 |
| 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: 2020-02-04, 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 Cited by 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: 32165585DOI: 10.1126/science.aaz2924 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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