1q16
From Proteopedia
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Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli
Overview
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.
About this Structure
1Q16 is a Protein complex structure of sequences from Escherichia coli with MD1, 6MO, HEM, SF4, F3S, AGA and 3PH as ligands. Active as Nitrate reductase, with EC number 1.7.99.4 Full crystallographic information is available from OCA.
Reference
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A., Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC, Nat Struct Biol. 2003 Sep;10(9):681-7. Epub 2003 Aug 10. PMID:12910261
Page seeded by OCA on Wed Nov 21 00:17:47 2007
Categories: Escherichia coli | Nitrate reductase | Protein complex | Bertero, M.G. | Strynadka, N.C.J. | 3PH | 6MO | AGA | F3S | HEM | MD1 | SF4 | Electron-transfer | Membrane protein
