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Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site.

DOI: 10.1074/jbc.M109.010058 DOI Help

Authors: Jonathan Ruprecht (MRC Mitocondrial Biology Unit) , Victoria Yankovskaya (Veterans Affairs Medical Center, the University of California) , Elena Maklashina (Veterans Affairs Medical Center University of California) , So Iwata (Diamond Light Source) , Gary Cecchini (Veterans Affairs Medical Center University of California)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry

State: Published (Approved)
Published: August 2009
Diamond Proposal Number(s): 316

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 Å 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.

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
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