Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 284, Issue 43, Pages 29836-29846Publisher
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DOI: 10.1074/jbc.M109.010058
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Funding
- National Institutes of Health [GM61606]
- Department of Veterans Affairs, Office of Research and Development, Biomedical Laboratory Research Division
- Human Receptor Crystallography Project, ERATO, Japan Science and Technology Agency [B17935]
- Biotechnology and Biological Sciences Research Council [BB/C505116/1, B17935] Funding Source: researchfish
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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 angstrom 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.
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