8Q0A
Inward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.
Summary for 8Q0A
| Entry DOI | 10.2210/pdb8q0a/pdb |
| EMDB information | 18051 |
| Descriptor | NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (59 entities in total) |
| Functional Keywords | complex i, oxidoreductase, proteoliposomes, membrane-bound, metabolism, membrane protein |
| Biological source | Bos taurus (cattle) More |
| Total number of polymer chains | 45 |
| Total formula weight | 1102682.55 |
| Authors | Grba, D.N.,Hirst, J. (deposition date: 2023-07-28, release date: 2024-06-05, Last modification date: 2024-06-26) |
| Primary citation | Grba, D.N.,Wright, J.J.,Yin, Z.,Fisher, W.,Hirst, J. Molecular mechanism of the ischemia-induced regulatory switch in mammalian complex I. Science, 384:1247-1253, 2024 Cited by PubMed Abstract: Respiratory complex I is an efficient driver for oxidative phosphorylation in mammalian mitochondria, but its uncontrolled catalysis under challenging conditions leads to oxidative stress and cellular damage. Ischemic conditions switch complex I from rapid, reversible catalysis into a dormant state that protects upon reoxygenation, but the molecular basis for the switch is unknown. We combined precise biochemical definition of complex I catalysis with high-resolution cryo-electron microscopy structures in the phospholipid bilayer of coupled vesicles to reveal the mechanism of the transition into the dormant state, modulated by membrane interactions. By implementing a versatile membrane system to unite structure and function, attributing catalytic and regulatory properties to specific structural states, we define how a conformational switch in complex I controls its physiological roles. PubMed: 38870289DOI: 10.1126/science.ado2075 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
Download full validation report
