Difference between revisions of "Part:BBa K346004"
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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.Function test of mercury MBP showed that our whole-cell bioabsorbents can absorb more than 50% of 10-6 M Hg (II) in 120 minutes, indicating that cells expressing certain metal binding peptide engineered via our method can decontaminate corresponding metal ion from aquatic environment. This design has been successfully applied to another homolog of MerR family – PbrR, the lead responsive regulator.In our project, we try to tandem two metal binding domains together to make a high performance and less energy consuming metal binding peptide. Our bacteria achieved an equivalent lead accumulation capacity as the mercury MBP, which proved validness of our engineering strategy. 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.Function test of mercury MBP showed that our whole-cell bioabsorbents can absorb more than 50% of 10-6 M Hg (II) in 120 minutes, indicating that cells expressing certain metal binding peptide engineered via our method can decontaminate corresponding metal ion from aquatic environment. This design has been successfully applied to another homolog of MerR family – PbrR, the lead responsive regulator.In our project, we try to tandem two metal binding domains together to make a high performance and less energy consuming metal binding peptide. Our bacteria achieved an equivalent lead accumulation capacity as the mercury MBP, which proved validness of our engineering strategy. This part works as the core part in the lead bioabsorption device. | ||
| − | [[Image:PbrR.jpg]] [[Image:lead | + | [[Image:PbrR.jpg]] [[Image:lead MBP1.jpg]] |
Revision as of 04:48, 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 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.Function test of mercury MBP showed that our whole-cell bioabsorbents can absorb more than 50% of 10-6 M Hg (II) in 120 minutes, indicating that cells expressing certain metal binding peptide engineered via our method can decontaminate corresponding metal ion from aquatic environment. This design has been successfully applied to another homolog of MerR family – PbrR, the lead responsive regulator.In our project, we try to tandem two metal binding domains together to make a high performance and less energy consuming metal binding peptide. Our bacteria achieved an equivalent lead accumulation capacity as the mercury MBP, which proved validness of our engineering strategy. This part works as the core part in the lead bioabsorption device.
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]