Amino-acid sequence of rusticyanin from Thiobacillus ferrooxidans and its comparison with other blue copper proteins.
Rusticyanin, a copper protein characterized by a high redox potential (+680 mV) and a high stability at acidic pH, is involved in iron oxidation in Thiobacillus ferrooxidans. It has been characterized from a new strain and its amino-acid sequence has been determined and compared to two other rusticyanin sequences isolated from different strains. It comprises 155 amino acids and the alignment of the three rusticyanins shows a high degree of homology. Comparing the rusticyanins with six blue copper proteins which have a copper-I site in common, a consensus sequence containing Cys, His and Met in the C-terminal part of the protein and His-85 is proposed to be involved in the copper coordination. Secondary structure predictions are compared to three structures of copper proteins obtained by X-ray crystallography.
Nunzi
F
F
Laboratoire de Chimie Bactérienne, CNRS, Marseille, France.
Woudstra
M
M
Campèse
D
D
Bonicel
J
J
Morin
D
D
Bruschi
M
M
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001400:Azurin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000302:isolation & purification; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D013855:Thiobacillus / Q000737:chemistry*
D000596:Amino Acids; C012543:rusticyanin; D001400:Azurin