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PDBsum entry 5d80
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Contents |
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(+ 0 more)
591 a.a.
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(+ 0 more)
457 a.a.
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445 a.a.
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104 a.a.
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216 a.a.
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203 a.a.
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88 a.a.
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81 a.a.
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178 a.a.
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68 a.a.
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223 a.a.
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212 a.a.
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115 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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Crystal structure of yeast V1-Atpase in the autoinhibited state.
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Authors
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R.A.Oot,
P.M.Kane,
E.A.Berry,
S.Wilkens.
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Ref.
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Embo J, 2016,
35,
1694-1706.
[DOI no: ]
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PubMed id
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Abstract
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Vacuolar ATPases (V-ATPases) are essential proton pumps that acidify the lumen
of subcellular organelles in all eukaryotic cells and the extracellular space in
some tissues. V-ATPase activity is regulated by a unique mechanism referred to
as reversible disassembly, wherein the soluble catalytic sector, V1, is released
from the membrane and its MgATPase activity silenced. The crystal structure of
yeast V1 presented here shows that activity silencing involves a large
conformational change of subunit H, with its C-terminal domain rotating ~150°
from a position near the membrane in holo V-ATPase to a position at the bottom
of V1 near an open catalytic site. Together with biochemical data, the structure
supports a mechanistic model wherein subunit H inhibits ATPase activity by
stabilizing an open catalytic site that results in tight binding of inhibitory
ADP at another site.
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