Part:BBa_K3425100
DNA Binding Domain-caffeine nanobody fusion protein
BioBrick created from the modular nanobody-based biosensor published by Chang et al (2018). It's composed (from N-ter to C-ter) of the E. coli CadC DNA binding domain, a juxtamembrane bridge region, an artificial 16L transmembrane region and the caffeine-binding camellid nanobody. The nanobody binds the target in a way that the protein CadC domains dimerize, which allows for the binding of the pCadBA operon region and promotes transcription downstream. The nanobody domain can be exchanged in order to bind to other targets. This gives this protein flexibility to choose potentially any target that has single domain antibodies available. The native CadC protein of E. coli is unlikely to promote unspecific transcription of pCadBA, but avoid using growth media with acid pH or high concentrations of lysine.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 56
Illegal BglII site found at 930 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 622
- 1000COMPATIBLE WITH RFC[1000]
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