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6VQ7

Mammalian V-ATPase from rat brain - composite model of rotational state 2 bound to ADP and SidK (built from focused refinement models)

Summary for 6VQ7
Entry DOI10.2210/pdb6vq7/pdb
EMDB information21318
DescriptorATPase H+-transporting V1 subunit A, ATPase, H+ transporting, V0 subunit B (Predicted), isoform CRA_a, V-type proton ATPase subunit S1, ... (18 entities in total)
Functional Keywordsmembrane protein complex, rotary atpase, proton transport
Biological sourceLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
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Total number of polymer chains34
Total formula weight1095887.44
Authors
Abbas, Y.M.,Rubinstein, J.L. (deposition date: 2020-02-04, release date: 2020-03-18, Last modification date: 2024-03-06)
Primary citationAbbas, 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: 32165585
DOI: 10.1126/science.aaz2924
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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