Difference between revisions of "Part:BBa K1980003"
Line 8: | Line 8: | ||
<partinfo>BBa_K1980003 SequenceAndFeatures</partinfo> | <partinfo>BBa_K1980003 SequenceAndFeatures</partinfo> | ||
− | + | ||
==Usage and Biology== | ==Usage and Biology== | ||
<p> Our project aimed to detect and chelate dietary copper as a treatment for Wilson's Disease, a copper accumulation disorder. | <p> Our project aimed to detect and chelate dietary copper as a treatment for Wilson's Disease, a copper accumulation disorder. |
Revision as of 12:56, 20 October 2016
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:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 595
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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.