Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Structure and activation mechanism of the hexameric plasma membrane H-ATPase.
Journal, issue, pages	Nat Commun, Vol. 12, Issue 1, Page 6439, Year 2021
Publish date	Nov 8, 2021
Authors	Peng Zhao / Chaoran Zhao / Dandan Chen / Caihong Yun / Huilin Li / Lin Bai /
PubMed Abstract	The S. cerevisiae plasma membrane H-ATPase, Pma1, is a P3A-type ATPase and the primary protein component of the membrane compartment of Pma1 (MCP). Like other plasma membrane H-ATPases, Pma1 ...The S. cerevisiae plasma membrane H-ATPase, Pma1, is a P3A-type ATPase and the primary protein component of the membrane compartment of Pma1 (MCP). Like other plasma membrane H-ATPases, Pma1 assembles and functions as a hexamer, a property unique to this subfamily among the larger family of P-type ATPases. It has been unclear how Pma1 organizes the yeast membrane into MCP microdomains, or why it is that Pma1 needs to assemble into a hexamer to establish the membrane electrochemical proton gradient. Here we report a high-resolution cryo-EM study of native Pma1 hexamers embedded in endogenous lipids. Remarkably, we found that the Pma1 hexamer encircles a liquid-crystalline membrane domain composed of 57 ordered lipid molecules. The Pma1-encircled lipid patch structure likely serves as the building block of the MCP. At pH 7.4, the carboxyl-terminal regulatory α-helix binds to the phosphorylation domains of two neighboring Pma1 subunits, locking the hexamer in the autoinhibited state. The regulatory helix becomes disordered at lower pH, leading to activation of the Pma1 hexamer. The activation process is accompanied by a 6.7 Å downward shift and a 40° rotation of transmembrane helices 1 and 2 that line the proton translocation path. The conformational changes have enabled us to propose a detailed mechanism for ATP-hydrolysis-driven proton pumping across the plasma membrane. Our structures will facilitate the development of antifungal drugs that target this essential protein.
External links	Nat Commun / PubMed:34750373 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.8 Å
Structure data	31986 7vh5 EMDB-31986, PDB-7vh5: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 7.4, C1 symmetry) Method: EM (single particle) / Resolution: 3.2 Å EMDB-31987: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 7.4, C6 symmetry) Method: EM (single particle) / Resolution: 2.9 Å 31988 7vh6 EMDB-31988, PDB-7vh6: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the active state (pH 6.0, BeF3-, conformation 1, C1 symmetry) Method: EM (single particle) / Resolution: 3.8 Å EMDB-31989: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the active state (pH 6.0, BeF3-, conformation 1, C6 symmetry) Method: EM (single particle) / Resolution: 3.4 Å EMDB-31990: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 6.0, BeF3-, conformation 2, C1 symmetry) Method: EM (single particle) / Resolution: 3.8 Å EMDB-31991: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 6.0, C1 symmetry) Method: EM (single particle) / Resolution: 3.8 Å EMDB-31992: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 6.0, high salt, C6 symmetry) Method: EM (single particle) / Resolution: 3.6 Å EMDB-31993: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 7.4, BeF3-, C6 symmetry) Method: EM (single particle) / Resolution: 3.8 Å
Chemicals	ChemComp-POV: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipidYM / POPC ChemComp-SPH: SPHINGOSINE / Sphingosine ChemComp-BEF*: BERYLLIUM TRIFLUORIDE ION
Source	Saccharomyces cerevisiae (brewer's yeast) saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
Keywords	TRANSLOCASE / P type ATPase / plasma membrane H+-ATPase / hexamer