1Y4Z
The crystal structure of Nitrate Reductase A, NarGHI, in complex with the Q-site inhibitor pentachlorophenol
Summary for 1Y4Z
Entry DOI | 10.2210/pdb1y4z/pdb |
Related | 1Q16 1SIW 1Y5I 1Y5L 1Y5N |
Descriptor | Respiratory nitrate reductase 1 alpha chain, PENTACHLOROPHENOL, Respiratory nitrate reductase 1 beta chain, ... (11 entities in total) |
Functional Keywords | nitrate reduction, electron transfer, membrane protein, q-site, oxidoreductase |
Biological source | Escherichia coli More |
Cellular location | Cell membrane; Peripheral membrane protein: P09152 P11349 Cell inner membrane; Multi-pass membrane protein: P11350 |
Total number of polymer chains | 3 |
Total formula weight | 229365.72 |
Authors | Bertero, M.G.,Rothery, R.A.,Boroumand, N.,Palak, M.,Blasco, F.,Ginet, N.,Weiner, J.H.,Strynadka, N.C.J. (deposition date: 2004-12-01, release date: 2005-03-08, Last modification date: 2024-10-30) |
Primary citation | Bertero, M.G.,Rothery, R.A.,Boroumand, N.,Palak, M.,Blasco, F.,Ginet, N.,Weiner, J.H.,Strynadka, N.C.J. Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A J.Biol.Chem., 280:14836-14843, 2005 Cited by PubMed Abstract: The crystal structure of Escherichia coli nitrate reductase A (NarGHI) in complex with pentachlorophenol has been determined to 2.0 A of resolution. We have shown that pentachlorophenol is a potent inhibitor of quinol:nitrate oxidoreductase activity and that it also perturbs the EPR spectrum of one of the hemes located in the membrane anchoring subunit (NarI). This new structural information together with site-directed mutagenesis data, biochemical analyses, and molecular modeling provide the first molecular characterization of a quinol binding and oxidation site (Q-site) in NarGHI. A possible proton conduction pathway linked to electron transfer reactions has also been defined, providing fundamental atomic details of ubiquinol oxidation by NarGHI at the bacterial membrane. PubMed: 15615728DOI: 10.1074/jbc.M410457200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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