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| [[Image:1q16.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1q16| PDB=1q16 | SCENE= }} | | {{STRUCTURE_1q16| PDB=1q16 | SCENE= }} |
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| '''Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli'''
| | ===Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli=== |
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| ==Overview==
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| The facultative anaerobe Escherichia coli is able to assemble specific respiratory chains by synthesis of appropriate dehydrogenases and reductases in response to the availability of specific substrates. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (nitrate reductase A; NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. We present here the crystal structure of NarGHI at a resolution of 1.9 A. The NarGHI structure identifies the number, coordination scheme and environment of the redox-active prosthetic groups, a unique coordination of the molybdenum atom, the first structural evidence for the role of an open bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) (Mo-bisMGD) cofactor in the catalytic mechanism and a novel fold of the membrane anchor subunit. Our findings provide fundamental molecular details for understanding the mechanism of proton-motive force generation by a redox loop. | | The line below this paragraph, {{ABSTRACT_PUBMED_12910261}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12910261 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12910261}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Electron-transfer]] | | [[Category: Electron-transfer]] |
| [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:44:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:19:06 2008'' |