Difference between revisions of "Part:BBa K4275026:Design"
 
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1. The export tag situated on the N terminal of the Neae-Nb3 fusion construct directs the transporation of the target protein to the outer membrane of the bacteria from periplasm.  
 
1. The export tag situated on the N terminal of the Neae-Nb3 fusion construct directs the transporation of the target protein to the outer membrane of the bacteria from periplasm.  
  
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2. The beta-barrel domain (Figure 1) in the Neae region spans accross the outer memrbane of E.Coli and provides structural support for the whole construct.
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2. The beta-barrel domain (Figure 1) in the Neae region spans accross the outer memrbane of <i>E.coli</i> and provides structural support for the whole construct.
  
 
3. A spacer domain is situated between the C terminal Nb3 domain and the transmembrane beta-barrel domain.
 
3. A spacer domain is situated between the C terminal Nb3 domain and the transmembrane beta-barrel domain.

Latest revision as of 01:12, 14 October 2022


Neae-Nb3


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]


Design Notes

1. The export tag situated on the N terminal of the Neae-Nb3 fusion construct directs the transporation of the target protein to the outer membrane of the bacteria from periplasm.

2. The beta-barrel domain (Figure 1) in the Neae region spans accross the outer memrbane of E.coli and provides structural support for the whole construct.

3. A spacer domain is situated between the C terminal Nb3 domain and the transmembrane beta-barrel domain.

Source

Escherichia coli (Neae)
Lama glama (Nb3)

References

1. Glass, David S, and Ingmar H Riedel-Kruse. “A Synthetic Bacterial Cell-Cell Adhesion Toolbox for Programming Multicellular Morphologies and Patterns.” Cell vol. 174,3 (2018): 649-658.e16. doi:10.1016/j.cell.2018.06.041