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-Structure paper
タイトル | High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane. |
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ジャーナル・号・ページ | Science, Vol. 360, Issue 6389, Year 2018 |
掲載日 | 2018年5月11日 |
著者 | Anurag P Srivastava / Min Luo / Wenchang Zhou / Jindrich Symersky / Dongyang Bai / Melissa G Chambers / José D Faraldo-Gómez / Maofu Liao / David M Mueller / |
PubMed 要旨 | 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- ...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. |
リンク | Science / PubMed:29650704 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 4.2 Å |
構造データ | EMDB-7546, PDB-6cp3: EMDB-7547, PDB-6cp5: |
化合物 | ChemComp-ATP: ChemComp-ADP: ChemComp-EFO: |
由来 |
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キーワード | BIOSYNTHETIC PROTEIN / ATP synthase |