PMID:8300624
| Citation |
Wülfing, C, Lombardero, J and Plückthun, A (1994) An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J. Biol. Chem. 269:2895-901 |
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| Abstract |
Initially detected as a persistent contaminant in immobilized metal affinity chromatography of recombinant proteins in Escherichia coli, a 196-amino acid protein was isolated, cloned, overexpressed, and characterized. It consists of two domains, of which the first (146 amino acids) shows some homology to the FK506-binding proteins. The second domain (50 amino acids) is extremely rich in potentially metal-binding amino acids, such as histidine, cysteine, and acidic amino acids. The protein binds Ni2+ and Zn2+ tightly with 1:1 stoichiometry, Cu2+ and Co2+ with lower affinity, and Mn2+, Fe2+, Fe3+, Mg2+, and Ca2+ hardly at all. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Carrier Proteins/chemistry; Cations, Divalent/analysis; Cations, Divalent/metabolism; Circular Dichroism; Computer Simulation; DNA Primers; Escherichia coli/metabolism; Heat-Shock Proteins/chemistry; Metals/metabolism; Models, Molecular; Molecular Sequence Data; Polymerase Chain Reaction/methods; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Tacrolimus Binding Proteins |
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