PMID:14725769
| Citation |
Jormakka, M, Richardson, D, Byrne, B and Iwata, S (2004) Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes. Structure 12:95-104 |
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| Abstract |
The structure of the catalytic and electron-transfer subunits (NarGH) of the integral membrane protein, respiratory nitrate reductase (Nar) has been determined to 2.0 A resolution revealing the molecular architecture of this Mo-bisMGD (molybdopterin-guanine-dinucleotide) containing enzyme which includes a previously undetected FeS cluster. Nar, together with the related enzyme formate dehydrogenase (Fdh-N), is a key enzyme in the generation of proton motive force across the membrane in Escherichia coli nitrate respiration. A comparative study revealed that Nar and Fdh-N employ different approaches for acquiring substrate, reflecting different catalytic mechanisms. Nar uses a very narrow and nonpolar substrate-conducting cavity with a nonspecific substrate binding site, whereas Fdh-N accommodates a wider, positively charged substrate-conducting cavity with a more specific substrate binding site. The Nar structure also demonstrates the first example of an Asp side chain acting as a Mo ligand providing a structural basis for the classification of Mo-bisMGD enzymes. |
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| Keywords |
Amino Acid Sequence; Catalysis; Catalytic Domain; Crystallography, X-Ray; Cysteine/chemistry; Electron Transport/physiology; Escherichia coli/enzymology; Formate Dehydrogenases/chemistry; Histidine/chemistry; Models, Molecular; Molecular Sequence Data; Molybdenum/chemistry; Nitrate Reductase; Nitrate Reductases/chemistry; Proton-Motive Force/physiology; Static Electricity |
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