6Q8X
Respiratory complex I from Thermus thermophilus with bound Pyridaben.
Summary for 6Q8X
| Entry DOI | 10.2210/pdb6q8x/pdb |
| Related | 6I0D 6I1P 6Q8O 6Q8W |
| Descriptor | NADH-quinone oxidoreductase subunit 1, NADH-quinone oxidoreductase subunit 7, NADH-quinone oxidoreductase subunit 10, ... (20 entities in total) |
| Functional Keywords | respiratory chain, complex i, nadh:ubiquinone oxidoreductase, electron transfer, proton translocation, membrane protein |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) More |
| Total number of polymer chains | 32 |
| Total formula weight | 1081307.11 |
| Authors | Gutierrez-Fernandez, J.,Minhas, G.S.,Sazanov, L.A. (deposition date: 2018-12-16, release date: 2020-09-02, Last modification date: 2024-10-23) |
| Primary citation | Gutierrez-Fernandez, J.,Kaszuba, K.,Minhas, G.S.,Baradaran, R.,Tambalo, M.,Gallagher, D.T.,Sazanov, L.A. Key role of quinone in the mechanism of respiratory complex I. Nat Commun, 11:4135-4135, 2020 Cited by PubMed Abstract: Complex I is the first and the largest enzyme of respiratory chains in bacteria and mitochondria. The mechanism which couples spatially separated transfer of electrons to proton translocation in complex I is not known. Here we report five crystal structures of T. thermophilus enzyme in complex with NADH or quinone-like compounds. We also determined cryo-EM structures of major and minor native states of the complex, differing in the position of the peripheral arm. Crystal structures show that binding of quinone-like compounds (but not of NADH) leads to a related global conformational change, accompanied by local re-arrangements propagating from the quinone site to the nearest proton channel. Normal mode and molecular dynamics analyses indicate that these are likely to represent the first steps in the proton translocation mechanism. Our results suggest that quinone binding and chemistry play a key role in the coupling mechanism of complex I. PubMed: 32811817DOI: 10.1038/s41467-020-17957-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.508 Å) |
Structure validation
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