8ESW
Structure of mitochondrial complex I from Drosophila melanogaster, Flexible-class 1
This is a non-PDB format compatible entry.
Summary for 8ESW
| Entry DOI | 10.2210/pdb8esw/pdb |
| EMDB information | 28581 28582 |
| Descriptor | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12, NADH-ubiquinone oxidoreductase chain 4, NADH-ubiquinone oxidoreductase chain 5, ... (52 entities in total) |
| Functional Keywords | nadh:ubiquinone oxidoreductase, translocase, oxidoreductase |
| Biological source | Drosophila melanogaster (fruit fly) More |
| Total number of polymer chains | 43 |
| Total formula weight | 1064010.03 |
| Authors | Padavannil, A.,Letts, J.A. (deposition date: 2022-10-15, release date: 2023-03-29, Last modification date: 2024-10-30) |
| Primary citation | Padavannil, A.,Murari, A.,Rhooms, S.K.,Owusu-Ansah, E.,Letts, J.A. Resting mitochondrial complex I from Drosophila melanogaster adopts a helix-locked state. Elife, 12:-, 2023 Cited by PubMed Abstract: Respiratory complex I is a proton-pumping oxidoreductase key to bioenergetic metabolism. Biochemical studies have found a divide in the behavior of complex I in metazoans that aligns with the evolutionary split between Protostomia and Deuterostomia. Complex I from Deuterostomia including mammals can adopt a biochemically defined off-pathway 'deactive' state, whereas complex I from Protostomia cannot. The presence of off-pathway states complicates the interpretation of structural results and has led to considerable mechanistic debate. Here, we report the structure of mitochondrial complex I from the thoracic muscles of the model protostome . We show that although complex I (-CI) does not have a NEM-sensitive deactive state, it does show slow activation kinetics indicative of an off-pathway resting state. The resting-state structure of -CI from the thoracic muscle reveals multiple conformations. We identify a helix-locked state in which an N-terminal α-helix on the NDUFS4 subunit wedges between the peripheral and membrane arms. Comparison of the -CI structure and conformational states to those observed in bacteria, yeast, and mammals provides insight into the roles of subunits across organisms, explains why the -CI off-pathway resting state is NEM insensitive, and raises questions regarding current mechanistic models of complex I turnover. PubMed: 36952377DOI: 10.7554/eLife.84415 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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