A [2Fe-2S] protein from the hyperthermophilic bacterium Aquifex aeolicus.
Overexpression in Escherichia coli of the fdx4 gene from Aquifex aeolicus has allowed isolation and characterization of the first hyperthermophilic [2Fe-2S](Scys)(4) protein, a homodimer of M = 2 x 12.4 kDa with one [2Fe-2S] cluster per subunit. This protein is undamaged by heating to 100 degrees C for at least three hours. The primary structure, in particular the characteristic distribution of the four cysteine ligands of the metal site, and the spectroscopic properties of the A. aeolicus protein relate it to well characterized [2Fe-2S] proteins from Clostridium pasteurianum and Azotobacter vinelandii. These proteins are also homologous to subunits or domains of hydrogenases and NADH-ubiquinone oxidoreductase (Complex I) of respiratory chains. The A. aeolicus [2Fe-2S] protein is thus representative of a presumably novel protein fold involved in a variety of functions in very diverse cellular backgrounds.
Chatelet
C
C
Département de Biologie Moléculaire et Structurale, CEA-Grenoble, Grenoble, 38054, France.
Gaillard
J
J
Pétillot
Y
Y
Louwagie
M
M
Meyer
J
J
D000595:Amino Acid Sequence; D016948:Azotobacter vinelandii / Q000737:chemistry; D001426:Bacterial Proteins; D001483:Base Sequence; D003013:Clostridium / Q000737:chemistry; D019281:Dimerization; D004355:Drug Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D016946:Gram-Negative Aerobic Rods and Cocci / Q000737:chemistry* / Q000235:genetics; D006358:Hot Temperature; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000235:genetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D011994:Recombinant Proteins; D016415:Sequence Alignment; D013053:Spectrophotometry
D001426:Bacterial Proteins; C120966:Fdx4 protein, Aquifex aeolicus; D007506:Iron-Sulfur Proteins; D011994:Recombinant Proteins