Difference between revisions of "Part:BBa K4035008"

 
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<partinfo>BBa_K4035008 short</partinfo>
 
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Copper metallotionein CUP1 (BBa_M45090) is a protein responsible for copper binding protein in the yeast Saccharomyces cerevisiae. In order to improve the copper fixation efficiency in yeast, CUP1 was linked to a second sequence of the same protein. The linker is a semi-rigid linker and is made of the GGGGS(EAAAK)2GGGGS amino acid sequences. GGGGS is flexible and (EAAAK)2 is rigid, making the linker rigid in the center with 2 flexible arms attached to the CUP1 proteins.  
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This protein is made of two yeast copper metallotionein protein, CUP1 (BBa_M45090), linked together by a semi-rigid linker made of the GGGGS(EAAAK)2GGGGS amino acid sequence.  
  
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===Usage and Biology===
 
===Usage and Biology===
  
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Copper metallotionein CUP1 (BBa_M45090) is a protein responsible for copper binding protein in the yeast Saccharomyces cerevisiae. In order to increase the copper retrieval efficiency, two copies of CUP1 were linked together and expressed at the outter surface of S. cerevisiae (BBa_K4035014). The linker is composed of two flexible regions GGGGS separated by two rigid regions EAAAK, making the linker rigid in the center with 2 flexible arms attached to the CUP1 proteins.
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<span class='h3bb'>Sequence and Features</span>
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===Characterization===
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===Sequence and Features===
 
<partinfo>BBa_K4035008 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4035008 SequenceAndFeatures</partinfo>
  

Revision as of 06:52, 13 September 2021


Dimerization of the copper metallothionein 1 : CUP1-GGGGS(EAAAK)2GGGGS-CUP1

This protein is made of two yeast copper metallotionein protein, CUP1 (BBa_M45090), linked together by a semi-rigid linker made of the GGGGS(EAAAK)2GGGGS amino acid sequence.

Usage and Biology

Copper metallotionein CUP1 (BBa_M45090) is a protein responsible for copper binding protein in the yeast Saccharomyces cerevisiae. In order to increase the copper retrieval efficiency, two copies of CUP1 were linked together and expressed at the outter surface of S. cerevisiae (BBa_K4035014). The linker is composed of two flexible regions GGGGS separated by two rigid regions EAAAK, making the linker rigid in the center with 2 flexible arms attached to the CUP1 proteins.

Characterization

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
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 391