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1Y5I

The crystal structure of the NarGHI mutant NarI-K86A

Summary for 1Y5I
Entry DOI10.2210/pdb1y5i/pdb
Related1Q16 1Y4Z 1Y5L 1Y5N
DescriptorRespiratory nitrate reductase 1 alpha chain, (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE, Respiratory nitrate reductase 1 beta chain, ... (11 entities in total)
Functional Keywordsnitrate reduction, membrane protein, electron transfer, q-site, oxidoreductase
Biological sourceEscherichia coli
More
Total number of polymer chains3
Total formula weight229834.18
Authors
Bertero, M.G.,Rothery, R.A.,Boroumand, N.,Palak, M.,Blasco, F.,Ginet, N.,Weiner, J.H.,Strynadka, N.C.J. (deposition date: 2004-12-02, release date: 2005-03-08, Last modification date: 2024-11-06)
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 (1.9 Å)
Structure validation

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