6ZIY

Respiratory complex I from Thermus thermophilus, NADH dataset, major state

Summary for 6ZIY

• Entry DOI: 10.2210/pdb6ziy/pdb
• EMDB information: 11231
• Descriptor: NADH-quinone oxidoreductase subunit 1, NADH-quinone oxidoreductase subunit 10, NADH-quinone oxidoreductase subunit 11, ... (19 entities in total)
• Functional Keywords: respiratory chain, complex i, nadh:ubiquinone oxidoreductase, electron transfer, proton translocation, membrane protein
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 15
• Total formula weight: 526752.45

Authors

Kaszuba, K.,Tambalo, M.,Gallagher, G.T.,Sazanov, L.A. (deposition date: 2020-06-26, release date: 2020-09-02, Last modification date: 2024-11-06)

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

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: 32811817
DOI: 10.1038/s41467-020-17957-0

Experimental method

ELECTRON MICROSCOPY (4.25 Å)