EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structure and activation mechanism of the hexameric plasma membrane H-ATPase.
ジャーナル・号・ページ	Nat Commun, Vol. 12, Issue 1, Page 6439, Year 2021
掲載日	2021年11月8日
著者	Peng Zhao / Chaoran Zhao / Dandan Chen / Caihong Yun / Huilin Li / Lin Bai /
PubMed 要旨	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.
リンク	Nat Commun / PubMed:34750373 / PubMed Central
手法	EM (単粒子)
解像度	2.9 - 3.8 Å
構造データ	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) 手法: EM (単粒子) / 解像度: 3.2 Å EMDB-31987: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 7.4, C6 symmetry) 手法: EM (単粒子) / 解像度: 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) 手法: EM (単粒子) / 解像度: 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) 手法: EM (単粒子) / 解像度: 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) 手法: EM (単粒子) / 解像度: 3.8 Å EMDB-31991: Cryo-EM structure of the hexameric plasma membrane H+-ATPase in the autoinhibited state (pH 6.0, C1 symmetry) 手法: EM (単粒子) / 解像度: 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) 手法: EM (単粒子) / 解像度: 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) 手法: EM (単粒子) / 解像度: 3.8 Å
化合物	ChemComp-POV: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / リン脂質YM / POホスファチジルコリン ChemComp-SPH: SPHINGOSINE / スフィンゴシン ChemComp-BEF*: BERYLLIUM TRIFLUORIDE ION
由来	Saccharomyces cerevisiae (パン酵母) saccharomyces cerevisiae (strain atcc 204508 / s288c) (パン酵母)
キーワード	TRANSLOCASE (輸送酵素) / P type ATPase / plasma membrane H+-ATPase / hexamer (オリゴマー)