5D80: Crystal Structure Of Yeast V1-atpase In The Autoinhibited Form

Citation:
Abstract
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 degrees 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.
PDB ID: 5D80Download
MMDB ID: 139877
PDB Deposition Date: 2015/8/14
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 6.2  Å
Source Organism:
Similar Structures:
Biological Unit for 5D80: pentadecameric; determined by author
Molecular Components in 5D80
Label Count Molecule
Proteins (15 molecules)
3
V-type Proton Atpase Catalytic Subunit a(Gene symbol: VMA1)
Molecule annotation
3
V-type Proton Atpase Subunit B(Gene symbol: VMA2)
Molecule annotation
1
V-type Proton Atpase Subunit H(Gene symbol: VMA13)
Molecule annotation
3
V-type Proton Atpase Subunit G(Gene symbol: VMA10)
Molecule annotation
3
V-type Proton Atpase Subunit E(Gene symbol: VMA4)
Molecule annotation
1
V-type Proton Atpase Subunit D(Gene symbol: VMA8)
Molecule annotation
1
V-type Proton Atpase Subunit F(Gene symbol: VMA7)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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