6Q9J

Crystal structure of reduced Aquifex aeolicus NADH-quinone oxidoreductase subunits NuoE G129S and NuoF bound to NADH

Summary for 6Q9J

• Entry DOI: 10.2210/pdb6q9j/pdb
• Related: 6Q9G
• Descriptor: NADH-quinone oxidoreductase subunit E, NADH-quinone oxidoreductase subunit F, FE2/S2 (INORGANIC) CLUSTER, ... (10 entities in total)
• Functional Keywords: respiratory chain, complex i, nadh ubiquinone oxidoreductase, fe-s clusters, oxidoreductase
• Biological source: Aquifex aeolicus (strain VF5); More
• Total number of polymer chains: 4
• Total formula weight: 138677.22

Authors

Wohlwend, D.,Gerhardt, S.,Gnandt, E.,Friedrich, T. (deposition date: 2018-12-18, release date: 2019-06-26, Last modification date: 2024-05-15)

Primary citation

Schulte, M.,Frick, K.,Gnandt, E.,Jurkovic, S.,Burschel, S.,Labatzke, R.,Aierstock, K.,Fiegen, D.,Wohlwend, D.,Gerhardt, S.,Einsle, O.,Friedrich, T.
A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.
Nat Commun, 10:2551-2551, 2019

PubMed Abstract: Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. In humans its dysfunction is associated with degenerative diseases. Here we report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with bound substrates in the reduced and oxidized states. The redox states differ by the flip of a peptide bond close to the NADH binding site. The orientation of this peptide bond is determined by the reduction state of the nearby [Fe-S] cluster N1a. Fixation of the peptide bond by site-directed mutagenesis led to an inactivation of electron transfer and a decreased reactive oxygen species (ROS) production. We suggest the redox-gated peptide flip to represent a previously unrecognized molecular switch synchronizing NADH oxidation in response to the redox state of the complex as part of an intramolecular feed-back mechanism to prevent ROS production.

PubMed: 31186428
DOI: 10.1038/s41467-019-10429-0

Experimental method

X-RAY DIFFRACTION (1.83 Å)