6N2Y の概要
| エントリーDOI | 10.2210/pdb6n2y/pdb |
| 関連するPDBエントリー | 6N2D 6N2Z 6N30 |
| EMDBエントリー | 9327 9333 9334 9335 9336 9337 9338 |
| 分子名称 | ATP synthase subunit alpha, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (13 entities in total) |
| 機能のキーワード | bacterial atp synthase, hydrolase |
| 由来する生物種 | Bacillus sp. (strain PS3) 詳細 |
| タンパク質・核酸の鎖数 | 22 |
| 化学式量合計 | 526601.98 |
| 構造登録者 | |
| 主引用文献 | Guo, H.,Suzuki, T.,Rubinstein, J.L. Structure of a bacterial ATP synthase. Elife, 8:-, 2019 Cited by PubMed Abstract: ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the PS3 ATP synthase in , purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme. PubMed: 30724163DOI: 10.7554/eLife.43128 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3 Å) |
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