An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif.
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.
Wülfing
C
C
Protein Engineering Group, Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
Lombardero
J
J
Plückthun
A
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D002413:Cations, Divalent / Q000032:analysis / Q000378:metabolism; D002942:Circular Dichroism; D003198:Computer Simulation; D017931:DNA Primers; D004926:Escherichia coli / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D008670:Metals / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction / Q000379:methods; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D022021:Tacrolimus Binding Proteins
D001426:Bacterial Proteins; D002352:Carrier Proteins; D002413:Cations, Divalent; D017931:DNA Primers; D006360:Heat-Shock Proteins; D008670:Metals; D011994:Recombinant Proteins; D022021:Tacrolimus Binding Proteins