2wdv | pdb_00002wdv

E. coli succinate:quinone oxidoreductase (SQR) with an empty quinone- binding pocket

spinqualitylabelsall models 2wdv, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wdv is a 12 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: F3S, FAD, FES, HEM, NA, SF4, TEO Related: 2wdq, 2wdr, 1nek, 1nen, 2acz Activity: Succinate dehydrogenase (quinone), with EC number 1.3.5.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DHSD_ECOLI] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [DHSA_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. [DHSC_ECOLI] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [DHSB_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site.,Ruprecht J, Yankovskaya V, Maklashina E, Iwata S, Cecchini G J Biol Chem. 2009 Oct 23;284(43):29836-46. Epub 2009 Aug 25. PMID:19710024 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Succinate Dehydrogenase

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