Summary for 6N2D
| Entry DOI | 10.2210/pdb6n2d/pdb |
| Related | 6N2Y 6N2Z 6N30 |
| EMDB information | 9327 9333 9334 9335 9336 9337 9338 |
| Descriptor | ATP synthase subunit b, ATP synthase subunit a, ATP synthase subunit c (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Bacillus sp. PS3 More |
| Total number of polymer chains | 13 |
| Total formula weight | 138325.42 |
| Authors | Guo, H.,Rubinstein, J.L. (deposition date: 2018-11-12, release date: 2019-02-20, Last modification date: 2024-03-20) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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