6O7X

Saccharomyces cerevisiae V-ATPase Stv1-V1VO State 3

6O7X の概要

• エントリーDOI: 10.2210/pdb6o7x/pdb
• 関連するPDBエントリー: 6O7T 6O7U 6O7V 6O7W
• EMDBエントリー: 0644 0645 0646 0647 0648
• 分子名称: V-type proton ATPase subunit C, V0 assembly protein 1, V-type proton ATPase subunit c'', ... (16 entities in total)
• 機能のキーワード: proton pump, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 31
• 化学式量合計: 1003723.94

構造登録者

Vasanthakumar, T.,Bueler, S.A.,Wu, D.,Beilsten-Edmands, V.,Robinson, C.V.,Rubinstein, J.L. (登録日: 2019-03-08, 公開日: 2019-04-03, 最終更新日: 2024-03-20)

主引用文献

Vasanthakumar, T.,Bueler, S.A.,Wu, D.,Beilsten-Edmands, V.,Robinson, C.V.,Rubinstein, J.L.
Structural comparison of the vacuolar and Golgi V-ATPases fromSaccharomyces cerevisiae.
Proc. Natl. Acad. Sci. U.S.A., 116:7272-7277, 2019

PubMed Abstract: Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification. In mammals, V-ATPase subunit isoforms are differentially targeted to various intracellular compartments or tissues, but how these subunit isoforms influence enzyme activity is not clear. In the yeast , isoform diversity is limited to two different versions of the proton-translocating subunit a: Vph1p, which is targeted to the vacuole, and Stv1p, which is targeted to the Golgi apparatus and endosomes. We show that purified V-ATPase complexes containing Vph1p have higher ATPase activity than complexes containing Stv1p and that the relative difference in activity depends on the presence of lipids. We also show that V complexes containing Stv1p could be readily purified without attached V regions. We used this effect to determine structures of the membrane-embedded V region with Stv1p at 3.1-Å resolution, which we compare with a structure of the V region with Vph1p that we determine to 3.2-Å resolution. These maps reveal differences in the surface charge near the cytoplasmic proton half-channel. Both maps also show the presence of bound lipids, as well as regularly spaced densities that may correspond to ergosterol or bound detergent, around the c-ring.

PubMed: 30910982
DOI: 10.1073/pnas.1814818116

実験手法

ELECTRON MICROSCOPY (8.7 Å)