Difference between revisions of "Part:BBa K1980002"
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MymT is a small prokaryotic copper metallothein discovered in <i>Mycobacterium tuberculosis</i>. It is believed that the protein may help the bacterium survive copper toxicity, though deleting the gene had no effect on pathogenicity in mice. It can bind up to 7 copper ions but has a preference for 4-6. Our version has a C terminal hexahistidine tag for purification and has been codon optimised for E. coli.
 
MymT is a small prokaryotic copper metallothein discovered in <i>Mycobacterium tuberculosis</i>. It is believed that the protein may help the bacterium survive copper toxicity, though deleting the gene had no effect on pathogenicity in mice. It can bind up to 7 copper ions but has a preference for 4-6. Our version has a C terminal hexahistidine tag for purification and has been codon optimised for E. coli.
  
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===Usage and Biology===
 
  
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K1980002 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1980002 SequenceAndFeatures</partinfo>
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==Usage and Biology==
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<p> Our project aimed to detect and chelate dietary copper as a treatment for Wilson's Disease, a copper accumulation disorder.
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We decided that the ideal copper chelation protein would have these properties:
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</p>
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<ul class="textLiFont">
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<li>Should be able to bind multiple copper ions per peptide to increase the efficient use of cell resources. </li>
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<li>They should be from the prokaryotic domain because eukaryotic proteins can have expression issues in <i>Escherichia coli.</i> </li>
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</ul>
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<p>
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MymT is a small prokaryotic metallothein discovered in <i>Mycobacterium tuberculosis</i> by Gold <i>et al.</i><sup>(1)</sup>. It is believed that the protein may help the bacterium survive copper toxicity.</p>
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<p> MymT is believed to bind up to 7 copper ions but has a preference for 4-6.<sup>(1)</sup>
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</p>
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<p>
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(1) Ben Gold, Haiteng Deng, Ruslana Bryk, Diana Vargas, David Eliezer, Julia Roberts,
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Xiuju Jiang, & Carl Nathan (2009) “Identification of a Copper-Binding Metallothionein in Pathogenic Mycobacteria” Nat Chem Biol.
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2008 October ; 4(10): 609–616. doi:10.1038/nchembio.109.</p>
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Revision as of 13:30, 20 October 2016


MymT

MymT is a small prokaryotic copper metallothein discovered in Mycobacterium tuberculosis. It is believed that the protein may help the bacterium survive copper toxicity, though deleting the gene had no effect on pathogenicity in mice. It can bind up to 7 copper ions but has a preference for 4-6. Our version has a C terminal hexahistidine tag for purification and has been codon optimised for E. coli.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 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.

MymT is a small prokaryotic metallothein discovered in Mycobacterium tuberculosis by Gold et al.(1). It is believed that the protein may help the bacterium survive copper toxicity.

MymT is believed to bind up to 7 copper ions but has a preference for 4-6.(1)

(1) Ben Gold, Haiteng Deng, Ruslana Bryk, Diana Vargas, David Eliezer, Julia Roberts, Xiuju Jiang, & Carl Nathan (2009) “Identification of a Copper-Binding Metallothionein in Pathogenic Mycobacteria” Nat Chem Biol. 2008 October ; 4(10): 609–616. doi:10.1038/nchembio.109.