Difference between revisions of "Part:BBa K346004"

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This part consists of  an RBS, a mbp which codes for the lead binding peptide and a terminator.
 
This part consists of  an RBS, a mbp which codes for the lead binding peptide and a terminator.
  
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===Description===
 
===Description===
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[[Image:MerR family.jpg]]
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MerR family TFs share a high similarity at the C-terminal metal binding domain , which indicates a similar metal recognition mechanism and metal-protein complex structure.Previous work shows that C-terminal metal binding domain can act as a metal accumulator without the help of the N-terminal DNA binding domain.Our work also show that the engineered MBP which is constructed from MerR can work properly. As a consequence, the lead Metal Binding Peptide engineered from PbrR, one member of the MerR family, can be designed and constructed in the similar way as the mercury MBP does.In our project, we try to tandem two metal binding domains together to make a high performance and less energy consuming metal binding peptide.This part works as the core part in the lead bioabsorption device.
 
MerR family TFs share a high similarity at the C-terminal metal binding domain , which indicates a similar metal recognition mechanism and metal-protein complex structure.Previous work shows that C-terminal metal binding domain can act as a metal accumulator without the help of the N-terminal DNA binding domain.Our work also show that the engineered MBP which is constructed from MerR can work properly. As a consequence, the lead Metal Binding Peptide engineered from PbrR, one member of the MerR family, can be designed and constructed in the similar way as the mercury MBP does.In our project, we try to tandem two metal binding domains together to make a high performance and less energy consuming metal binding peptide.This part works as the core part in the lead bioabsorption device.
  
[[Image:PbrR.jpg]]      [[Image:lead PbrR1.jpg]]
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[[Image:lead mbd1.jpg]]
  
  
  
The figure shows the structure of PbrR and MBP(lead). The left figure is PbrR, the lead-responsive transcription factor,one member of MerR family. The right figure shows the predicted structure of resulted metal binding peptide of lead. lead ions are indicated as black balls in metal binding pockets.
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The figure shows the structure ofMBP(lead). The figure shows the predicted structure of resulted metal binding peptide of lead, which is engineered from PbrR, a member of MerR family. lead ions are indicated as black balls in metal binding pockets.
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Revision as of 01:48, 25 October 2010

RBS(B0034)_MBP(lead metal binding peptide egineered from PbrR)+Terminator(B0015)

This part consists of an RBS, a mbp which codes for the lead binding peptide and a terminator.


Description

MerR family.jpg


MerR family TFs share a high similarity at the C-terminal metal binding domain , which indicates a similar metal recognition mechanism and metal-protein complex structure.Previous work shows that C-terminal metal binding domain can act as a metal accumulator without the help of the N-terminal DNA binding domain.Our work also show that the engineered MBP which is constructed from MerR can work properly. As a consequence, the lead Metal Binding Peptide engineered from PbrR, one member of the MerR family, can be designed and constructed in the similar way as the mercury MBP does.In our project, we try to tandem two metal binding domains together to make a high performance and less energy consuming metal binding peptide.This part works as the core part in the lead bioabsorption device.

Lead mbd1.jpg


The figure shows the structure ofMBP(lead). The figure shows the predicted structure of resulted metal binding peptide of lead, which is engineered from PbrR, a member of MerR family. lead ions are indicated as black balls in metal binding pockets.


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]