2WDR
E. coli succinate:quinone oxidoreductase (SQR) with pentachlorophenol bound
Summary for 2WDR
| Entry DOI | 10.2210/pdb2wdr/pdb |
| Related | 1NEK 1NEN 2ACZ 2WDQ 2WDV |
| Descriptor | SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT, FE3-S4 CLUSTER, PROTOPORPHYRIN IX CONTAINING FE, ... (12 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 |
| Biological source | ESCHERICHIA COLI More |
| Cellular location | Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : P0AC41 Cell inner membrane ; Peripheral membrane protein : P07014 Cell inner membrane; Multi-pass membrane protein: P69054 P0AC44 |
| Total number of polymer chains | 12 |
| Total formula weight | 363413.72 |
| Authors | Ruprecht, J.,Yankovskaya, V.,Maklashina, E.,Iwata, S.,Cecchini, G. (deposition date: 2009-03-25, release date: 2009-08-25, Last modification date: 2015-02-04) |
| 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-, 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 (3.2 Å) |
Structure validation
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