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1Y4Z

The crystal structure of Nitrate Reductase A, NarGHI, in complex with the Q-site inhibitor pentachlorophenol

Summary for 1Y4Z
Entry DOI10.2210/pdb1y4z/pdb
Related1Q16 1SIW 1Y5I 1Y5L 1Y5N
DescriptorRespiratory nitrate reductase 1 alpha chain, PENTACHLOROPHENOL, Respiratory nitrate reductase 1 beta chain, ... (11 entities in total)
Functional Keywordsnitrate reduction, electron transfer, membrane protein, q-site, oxidoreductase
Biological sourceEscherichia coli
More
Cellular locationCell membrane; Peripheral membrane protein: P09152 P11349
Cell inner membrane; Multi-pass membrane protein: P11350
Total number of polymer chains3
Total formula weight229365.72
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 citationBertero, 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: 15615728
DOI: 10.1074/jbc.M410457200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

237735

數據於2025-06-18公開中

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