1Q16

Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli

Summary for 1Q16

• Entry DOI: 10.2210/pdb1q16/pdb
• Descriptor: Respiratory nitrate reductase 1 alpha chain, PROTOPORPHYRIN IX CONTAINING FE, Respiratory nitrate reductase 1 beta chain, ... (11 entities in total)
• Functional Keywords: membrane protein, electron-transfer, 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: 230023.47

Authors

Bertero, M.G.,Strynadka, N.C.J. (deposition date: 2003-07-18, release date: 2003-10-07, Last modification date: 2024-10-30)

Primary citation

Bertero, M.G.,Rothery, R.A.,Palak, M.,Hou, C.,Lim, D.,Blasco, F.,Weiner, J.H.,Strynadka, N.C.J.
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
Nat.Struct.Biol., 10:681-687, 2003

PubMed Abstract: 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.

PubMed: 12910261
DOI: 10.1038/nsb969

Experimental method

X-RAY DIFFRACTION (1.9 Å)