9BPB
Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae
Summary for 9BPB
| Entry DOI | 10.2210/pdb9bpb/pdb |
| EMDB information | 44770 |
| Descriptor | Cytochrome b-c1 complex subunit 1, mitochondrial, Cytochrome b-c1 complex subunit 10, mitochondrial, Cytochrome c oxidase subunit 1, ... (40 entities in total) |
| Functional Keywords | complex, oxidoreductase, respiration, electron transport |
| Biological source | Saccharomyces cerevisiae W303 More |
| Total number of polymer chains | 42 |
| Total formula weight | 990971.51 |
| Authors | Eldeeb, M.H.,Carlstrom, A.,Berndtsson, J.,Ott, M.,Fontanesi, F. (deposition date: 2024-05-07, release date: 2025-05-21, Last modification date: 2026-06-17) |
| Primary citation | Eldeeb, M.H.,Cosner, Z.,Carlstrom, A.,Mays, J.N.,Rodriguez, G.F.,Berndtsson, J.,Ott, M.,Fontanesi, F. Mitochondrial respirasome-like supercomplexes support metabolic flexibility in yeast. Nat Commun, 2026 Cited by PubMed Abstract: The mitochondrial respiratory chain (MRC) complexes, crucial for aerobic energy transduction in eukaryotes, form conserved higher-order structures called supercomplexes (SCs). The elucidation of SC physiological relevance is critical for our understanding of mitochondrial function and bioenergetics but has been hindered by the limited availability of experimental models isolating SC formation as the sole variable. In baker's yeast, SCs comprise IIIIV and IIIIV configurations, which enhance respiratory rates by facilitating cytochrome c diffusion along the SC surface. However, the roles of distinct SC conformations and MRC plasticity remain unclear. To address these questions, we engineered a yeast strain expressing a covalently-linked IIIIV SC, structurally like the wild-type. Expression of this tethered SC supports robust respiratory activity but selectively impacts cytosolic NADH-driven respiration, due to distinct interactions with the NADH dehydrogenase Nde1. We propose that in yeast mitochondria, substrate-specific respirasome-like SCs contribute to the optimization of electron fluxes and support metabolic flexibility. PubMed: 42014734DOI: 10.1038/s41467-026-72228-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.57 Å) |
Structure validation
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