6r7p | pdb_00006r7p

Crystal structure of oxidized Aquifex aeolicus NADH-quinone oxidoreductase subunits NuoE and NuoF S96M

spinqualitylabelsall models 6r7p, resolution 3.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r7p is a 4 chain structure with sequence from Aquifex aeolicus and Aquifex aeolicus VF5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.22Å Ligands: CL, FES, FMN, NA, SF4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NUOE_AQUAE NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). Publication Abstract from PubMed 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 A 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. A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.,Schulte M, Frick K, Gnandt E, Jurkovic S, Burschel S, Labatzke R, Aierstock K, Fiegen D, Wohlwend D, Gerhardt S, Einsle O, Friedrich T Nat Commun. 2019 Jun 11;10(1):2551. doi: 10.1038/s41467-019-10429-0. PMID:31186428 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NADH-quinone oxidoreductase

Proteopedia Page Contributors and Editors (what is this?)

OCA