5BW9

Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form

Summary for 5BW9

• Entry DOI: 10.2210/pdb5bw9/pdb
• Descriptor: V-type proton ATPase catalytic subunit A, V-type proton ATPase subunit B, V-type proton ATPase subunit H, ... (6 entities in total)
• Functional Keywords: hydrolase, autoinhibition
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 28
• Total formula weight: 1162568.89

Authors

Oot, R.A.,Kane, P.M.,Berry, E.A.,Wilkens, S. (deposition date: 2015-06-06, release date: 2016-06-08, Last modification date: 2023-09-27)

Primary citation

Oot, R.A.,Kane, P.M.,Berry, E.A.,Wilkens, S.
Crystal structure of yeast V1-ATPase in the autoinhibited state.
Embo J., 35:1694-1706, 2016

PubMed 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° 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.

PubMed: 27295975
DOI: 10.15252/embj.201593447

Experimental method

X-RAY DIFFRACTION (7 Å)