Part:BBa_K1980003

MymT sfGFP

MymT is a small prokaryotic copper metallothein discovered in Mycobacterium tuberculosis. It can bind up to 7 copper ions but has a preference for 4-6. This version has a C terminal sfGFP with a C terminal hexahistidine tag for purification. The MymT and sfGFP are separated by a short hydrophilic, flexible linker. This part has been codon optimised for E. coli.

Sequence and Features:

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal XhoI site found at 595
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

Usage and Biology

Our project aimed to detect and chelate dietary copper as a treatment for Wilson's Disease, a copper accumulation disorder. We decided that the ideal copper chelation protein would have these properties:

• Should be able to bind multiple copper ions per peptide to increase the efficient use of cell resources.
• They should be from the prokaryotic domain because eukaryotic proteins can have expression issues in Escherichia coli.

It is believed that the protein may help the bacterium survive copper toxicity, though deleting the gene had no effect on pathogenicity in mice.