7AWT
E. coli NADH quinone oxidoreductase hydrophilic arm
Summary for 7AWT
| Entry DOI | 10.2210/pdb7awt/pdb |
| EMDB information | 11930 |
| Descriptor | NADH-quinone oxidoreductase subunit B, FLAVIN MONONUCLEOTIDE, NADH-quinone oxidoreductase subunit C/D, ... (11 entities in total) |
| Functional Keywords | e. coli, respiratory complex i, electron transport |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 6 |
| Total formula weight | 285816.02 |
| Authors | Schimpf, J.,Grishkovskaya, I.,Haselbach, D.,Friedrich, T. (deposition date: 2020-11-09, release date: 2021-09-15, Last modification date: 2024-07-10) |
| Primary citation | Schimpf, J.,Oppermann, S.,Gerasimova, T.,Santos Seica, A.F.,Hellwig, P.,Grishkovskaya, I.,Wohlwend, D.,Haselbach, D.,Friedrich, T. Structure of the peripheral arm of a minimalistic respiratory complex I. Structure, 30:80-, 2022 Cited by PubMed Abstract: Respiratory complex I drives proton translocation across energy-transducing membranes by NADH oxidation coupled with (ubi)quinone reduction. In humans, its dysfunction is associated with neurodegenerative diseases. The Escherichia coli complex represents the structural minimal form of an energy-converting NADH:ubiquinone oxidoreductase. Here, we report the structure of the peripheral arm of the E. coli complex I consisting of six subunits, the FMN cofactor, and nine iron-sulfur clusters at 2.7 Å resolution obtained by cryo electron microscopy. While the cofactors are in equivalent positions as in the complex from other species, individual subunits are adapted to the absence of supernumerary proteins to guarantee structural stability. The catalytically important subunits NuoC and D are fused resulting in a specific architecture of functional importance. Striking features of the E. coli complex are scrutinized by mutagenesis and biochemical characterization of the variants. Moreover, the arrangement of the subunits sheds light on the unknown assembly of the complex. PubMed: 34562374DOI: 10.1016/j.str.2021.09.005 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.73 Å) |
Structure validation
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