Summary for 8E73
| Entry DOI | 10.2210/pdb8e73/pdb |
| EMDB information | 27934 28798 29088 29089 29090 29091 29092 29093 29094 29095 |
| Descriptor | MPP-beta, QCR10 (UCRY), MPP-alpha (protomer 2), ... (72 entities in total) |
| Functional Keywords | respiratory supercomplex, nadh-cyt c oxidoreductase, membrane complex, electron transport |
| Biological source | Vigna radiata More |
| Total number of polymer chains | 68 |
| Total formula weight | 1622406.25 |
| Authors | Maldonado, M.,Letts, J.A. (deposition date: 2022-08-23, release date: 2023-01-11, Last modification date: 2023-02-08) |
| Primary citation | Maldonado, M.,Fan, Z.,Abe, K.M.,Letts, J.A. Plant-specific features of respiratory supercomplex I + III 2 from Vigna radiata. Nat.Plants, 9:157-168, 2023 Cited by PubMed Abstract: The last steps of cellular respiration-an essential metabolic process in plants-are carried out by mitochondrial oxidative phosphorylation. This process involves a chain of multi-subunit membrane protein complexes (complexes I-V) that form higher-order assemblies called supercomplexes. Although supercomplexes are the most physiologically relevant form of the oxidative phosphorylation complexes, their functions and structures remain mostly unknown. Here we present the cryogenic electron microscopy structure of the supercomplex I + III from Vigna radiata (mung bean). The structure contains the full subunit complement of complex I, including a newly assigned, plant-specific subunit. It also shows differences in the mitochondrial processing peptidase domain of complex III relative to a previously determined supercomplex with complex IV. The supercomplex interface, while reminiscent of that in other organisms, is plant specific, with a major interface involving complex III's mitochondrial processing peptidase domain and no participation of complex I's bridge domain. The complex I structure suggests that the bridge domain sets the angle between the enzyme's two arms, limiting large-scale conformational changes. Moreover, complex I's catalytic loops and its response in active-to-deactive assays suggest that, in V. radiata, the resting complex adopts a non-canonical state and can sample deactive- or open-like conformations even in the presence of substrate. This study widens our understanding of the possible conformations and behaviour of complex I and supercomplex I + III. Further studies of complex I and its supercomplexes in diverse organisms are needed to determine the universal and clade-specific mechanisms of respiration. PubMed: 36581760DOI: 10.1038/s41477-022-01306-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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