8X02
E2 core of 2-oxoglutarate dehydrogenase complex
Summary for 8X02
| Entry DOI | 10.2210/pdb8x02/pdb |
| EMDB information | 37965 |
| Descriptor | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (1 entity in total) |
| Functional Keywords | structure of mitochondrial enzyme complex, transferase |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 24 |
| Total formula weight | 1176923.62 |
| Authors | |
| Primary citation | Zhang, Y.,Chen, M.,Chen, X.,Zhang, M.,Yin, J.,Yang, Z.,Gao, X.,Zhang, S.,Yang, M. Molecular architecture of the mammalian 2-oxoglutarate dehydrogenase complex. Nat Commun, 15:8407-8407, 2024 Cited by PubMed Abstract: The 2-oxoglutarate dehydrogenase complex (OGDHc) orchestrates a critical reaction regulating the TCA cycle. Although the structure of each OGDHc subunit has been solved, the architecture of the intact complex and inter-subunit interactions still remain unknown. Here we report the assembly of native, intact OGDHc from Sus scrofa heart tissue using cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), and subtomogram averaging (STA) to discern native structures of the whole complex and each subunit. Our cryo-EM analyses revealed the E2o cubic core structure comprising eight homotrimers at 3.3-Å resolution. More importantly, the numbers, positions and orientations of each OGDHc subunit were determined by cryo-ET and the STA structures of the core were resolved at 7.9-Å with the peripheral subunits reaching nanometer resolution. Although the distribution of the peripheral subunits E1o and E3 vary among complexes, they demonstrate a certain regularity within the position and orientation. Moreover, we analyzed and validated the interactions between each subunit, and determined the flexible binding mode for E1o, E2o and E3, resulting in a proposed model of Sus scrofa OGDHc. Together, our results reveal distinctive factors driving the architecture of the intact, native OGDHc. PubMed: 39333186DOI: 10.1038/s41467-024-52792-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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