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PDBsum entry 6vqc
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Proton transport
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PDB id
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6vqc
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Contents |
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104 a.a.
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110 a.a.
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441 a.a.
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203 a.a.
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41 a.a.
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350 a.a.
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78 a.a.
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84 a.a.
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(+ 3 more)
150 a.a.
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52 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure of V-Atpase from the mammalian brain.
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Authors
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Y.M.Abbas,
D.Wu,
S.A.Bueler,
C.V.Robinson,
J.L.Rubinstein.
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Ref.
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Science, 2020,
367,
1240-1246.
[DOI no: ]
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PubMed id
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Abstract
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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 Legionella pneumophila 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.
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