7NY1

Structure of the fungal plasma membrane proton pump Pma1 in its auto-inhibited state - hexameric assembly

Summary for 7NY1

• Entry DOI: 10.2210/pdb7ny1/pdb
• Related: 7NXF
• EMDB information: 12644
• Descriptor: Plasma membrane ATPase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: membrane protein, p-type atpase, proton-transporting atpase, proton transport
• Biological source: Neurospora crassa
• Total number of polymer chains: 6
• Total formula weight: 602849.78

Authors

Heit, S.,Geurts, M.M.G.,Murphy, B.J.,Corey, R.,Mills, D.J.,Kuehlbrandt, W.,Bublitz, M. (deposition date: 2021-03-19, release date: 2021-11-17, Last modification date: 2024-07-10)

Primary citation

Heit, S.,Geurts, M.M.G.,Murphy, B.J.,Corey, R.A.,Mills, D.J.,Kuhlbrandt, W.,Bublitz, M.
Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state.
Sci Adv, 7:eabj5255-eabj5255, 2021

PubMed Abstract: The fungal plasma membrane H-ATPase Pma1 is a vital enzyme, generating a proton-motive force that drives the import of essential nutrients. Autoinhibited Pma1 hexamers in the plasma membrane of starving fungi are activated by glucose signaling and subsequent phosphorylation of the autoinhibitory domain. As related P-type adenosine triphosphatases (ATPases) are not known to oligomerize, the physiological relevance of Pma1 hexamers remained unknown. We have determined the structure of hexameric Pma1 from by electron cryo-microscopy at 3.3-Å resolution, elucidating the molecular basis for hexamer formation and autoinhibition and providing a basis for structure-based drug development. Coarse-grained molecular dynamics simulations in a lipid bilayer suggest lipid-mediated contacts between monomers and a substantial protein-induced membrane deformation that could act as a proton-attracting funnel.

PubMed: 34757782
DOI: 10.1126/sciadv.abj5255

Experimental method

ELECTRON MICROSCOPY (3.26 Å)