Coding

Part:BBa_K5143008

Designed by: Aymeric Perrel   Group: iGEM24_UnivLyon1-INSALyon   (2024-07-30)
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ScCBD_cex'V2 : a Cellulose Binding Domain, that enables the fixation of proteins to Cellulose


Protein Description

Description

ScCBD_cex'V2 (Cellulose Binding Domain) is a peptide that has a huge affinity for bacterial cellulose. When fused with another protein, ScCBD_cex'V2 enables the fixation of the protein on the bacterial cellulose. This version of ScCBD_Cex has been modified to avoid recombination with ScCBD_Cex'V1 in the yeast.

CBD_CexV2
Figure 1: ScCBD_Cex'V2 three-dimensional structure
Functional cellulose
Figure 2: Functional cellulose
ScCBD_Cex coding sequence
Figure 3: ScCBD_Cex coding sequence

Construction

ScCBD-Cex'V2 was synthesised and its nucleotide sequence optimised for synthesis and expression in Saccharomyces cerevisiae. This optimised sequence has been modified to avoid recombination with ScCBD-Cex'V1 in the Yeast. ScCDB-Cex'V2 protein is used in fusion with bioglue composite biobrick (Cp19k_MaSp1) in order to functionalise bacterial cellulose with sticky properties: BBa_K5143022


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 256
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 226
    Illegal AgeI site found at 265
  • 1000
    COMPATIBLE WITH RFC[1000]


References

Ong, E., Gilkes, N. R., Miller, R. C., Warren, R. A. & Kilburn, D. G. Te cellulose-binding domain (CBD(Cex)) of an exoglucanase from Cellulomonas fmi: production in Escherichia coli and characterization of the polypeptide. Biotechnol. Bioeng. 42, 401–409 (1993).

Gilbert, C.; Tang, T.-C.; Ott, W.; Dorr, B. A.; Shaw, W. M.; Sun, G. L.; Lu, T. K.; Ellis, T. Living Materials with Programmable Functionalities Grown from Engineered Microbial Co-Cultures. Nat. Mater. 2021, 20 (5), 691–700. https://doi.org/10.1038/s41563-020-00857-5.


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