6CP3

Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc with inhibitor of oligomycin bound.

6CP3 の概要

• エントリーDOI: 10.2210/pdb6cp3/pdb
• EMDBエントリー: 7546
• 分子名称: ATP synthase subunit 9, mitochondrial, ATP synthase subunit H, mitochondrial, ATP synthase subunit f, mitochondrial, ... (16 entities in total)
• 機能のキーワード: atp synthase, biosynthetic protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 27
• 化学式量合計: 573364.21

構造登録者

Srivastava, A.P.,Luo, M.,Symersky, J.,Liao, M.F.,Mueller, D.M. (登録日: 2018-03-13, 公開日: 2018-04-11, 最終更新日: 2024-10-09)

主引用文献

Srivastava, A.P.,Luo, M.,Zhou, W.,Symersky, J.,Bai, D.,Chambers, M.G.,Faraldo-Gomez, J.D.,Liao, M.,Mueller, D.M.
High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.
Science, 360:-, 2018

PubMed Abstract: Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded F motor that rotates to drive ATP synthesis in the F subunit. We used single-particle cryo-electron microscopy (cryo-EM) to obtain structures of the full complex in a lipid bilayer in the absence or presence of the inhibitor oligomycin at 3.6- and 3.8-angstrom resolution, respectively. To limit conformational heterogeneity, we locked the rotor in a single conformation by fusing the F6 subunit of the stator with the δ subunit of the rotor. Assembly of the enzyme with the F6-δ fusion caused a twisting of the rotor and a 9° rotation of the F c-ring in the direction of ATP synthesis, relative to the structure of isolated F Our cryo-EM structures show how F and F are coupled, give insight into the proton translocation pathway, and show how oligomycin blocks ATP synthesis.

PubMed: 29650704
DOI: 10.1126/science.aas9699

実験手法

ELECTRON MICROSCOPY (3.8 Å)