2WDQ
E. coli succinate:quinone oxidoreductase (SQR) with carboxin bound
Summary for 2WDQ
| Entry DOI | 10.2210/pdb2wdq/pdb |
| Related | 1NEK 1NEN 2ACZ 2WDR |
| Descriptor | SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (14 entities in total) |
| Functional Keywords | succinate dehydrogenase activity, cell inner membrane, tricarboxylic acid cycle, cell membrane, metal-binding, transmembrane, transport, iron-sulfur, flavoprotein, oxidoreductase, electron transport, fad, iron, heme, membrane |
| Biological source | ESCHERICHIA COLI More |
| Total number of polymer chains | 12 |
| Total formula weight | 363608.81 |
| Authors | Ruprecht, J.,Yankovskaya, V.,Maklashina, E.,Iwata, S.,Cecchini, G. (deposition date: 2009-03-25, release date: 2009-08-25, Last modification date: 2024-10-23) |
| Primary citation | Ruprecht, J.,Yankovskaya, V.,Maklashina, E.,Iwata, S.,Cecchini, G. Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site. J. Biol. Chem., 284:29836-29846, 2009 Cited by PubMed Abstract: Three new structures of Escherichia coli succinate-quinone oxidoreductase (SQR) have been solved. One with the specific quinone-binding site (Q-site) inhibitor carboxin present has been solved at 2.4 A resolution and reveals how carboxin inhibits the Q-site. The other new structures are with the Q-site inhibitor pentachlorophenol and with an empty Q-site. These structures reveal important details unresolved in earlier structures. Comparison of the new SQR structures shows how subtle rearrangements of the quinone-binding site accommodate the different inhibitors. The position of conserved water molecules near the quinone binding pocket leads to a reassessment of possible water-mediated proton uptake networks that complete reduction of ubiquinone. The dicarboxylate-binding site in the soluble domain of SQR is highly similar to that seen in high resolution structures of avian SQR (PDB 2H88) and soluble flavocytochrome c (PDB 1QJD) showing mechanistically significant structural features conserved across prokaryotic and eukaryotic SQRs. PubMed: 19710024DOI: 10.1074/jbc.M109.010058 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
