Part:BBa_K2310998
Metal Binding Protein
Metallothioneins (MTs) is a novel kind of sulfur-based metal clusters. MTs contains some 200 amino acid residues, among them 20 Cys, and binding a total of 7 equiv of bivalent metal ions. Aromatic amino acid residues are absent. All Cys occur in the reduced form and are coordinated to the metal ions through mercaptide bonds. The abundance of Cys and their conspicuous arrangement in chelating Cys-Cys, Cys-X-Cys, and Cys-X-Y-Cys, where X and Y are residues other than Cys, predispose MT toward the binding of “soft” metal ions. Amino acid sequences are now known for over 36 class I MTs, for 4 class I1 MTs, and for 2 homologous sets of class 111MTs. So, in order to minimize the toxic effects of metals on E. coli, metallothionein can be used as a part in the future work. One of the most common metallothionein in the prokaryotes is designed as this part.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 106
- 1000COMPATIBLE WITH RFC[1000]
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