Wülfing C, Lombardero J, Plückthun A
Protein Engineering Group, Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
J Biol Chem. 1994 Jan 28;269(4):2895-901.
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.
最初，在大肠杆菌中重组蛋白的固定化金属亲和层析过程中，一种196个氨基酸的蛋白质被检测为持久性污染物，随后该蛋白质被分离、克隆、过量表达并进行了表征。它由两个结构域组成，其中第一个结构域（146个氨基酸）与FK506结合蛋白有一定同源性。第二个结构域（50个氨基酸）富含潜在的金属结合氨基酸，如组氨酸、半胱氨酸和酸性氨基酸。该蛋白质以1:1的化学计量比紧密结合Ni2+和Zn2+，与Cu2+和Co2+的亲和力较低，几乎不结合Mn2+、Fe2+、Fe3+、Mg2+和Ca2+。
