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     <title>Protein Description</title>
 
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     <h1>Description</h1>
 
     <h1>Description</h1>
 
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         ECRIRE DES TRUCS ICI POUR LA DESCRIPTION
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         ScCBD_cex'V1 (Cellulose Binding Domain) is a peptide that has a huge affinity for bacterial cellulose. When fused with another protein, ScCBD_cex'V1 enables the fixation of the protein on the bacterial cellulose.
 
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     <img src="https://static.igem.wiki/teams/5143/backbone-plasmid-bba-k5143005.png" width="400" alt="NOM PHOTO">
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            <img src="https://static.igem.wiki/teams/5143/bba-k5143007-cbd-cexv1-1.png" width="200" alt="CBD_CexV1">
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            <figcaption><i><u>Figure 1:</u> ScCBD_Cex'V1 three-dimensional structure</i></figcaption>
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            <img src="https://static.igem.wiki/teams/5143/bba-k5143007-cbd-cexv1-2.png" width="400" alt="Functional cellulose">
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            <figcaption><i><u>Figure 2:</u> Functional cellulose</i></figcaption>
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            <img src="https://static.igem.wiki/teams/5143/bba-k5143007-cbd-cexv1-3.png" width="100" alt="ScCBD_Cex coding sequence">
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            <figcaption><i><u>Figure 3:</u> ScCBD_Cex coding sequence</i></figcaption>
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     <h1>Construction</h1>
 
     <h1>Construction</h1>
 
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       ScCBD-Cex'V1 was synthesised and its nucleotide sequence optimised for synthesis and expression in <i>Saccharomyces cerevisiae</i>. ScCDB-Cex'V1 protein is used in fusion with bioglue composite biobrick (Cp19k_MaSp1) in order to functionalise bacterial cellulose with sticky properties: <a href="https://parts.igem.org/Part:BBa_K5143022" target="_blank">BBa_K5143022</a>
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    <h1>References</h1>
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<span class='h3bb'>Sequence and Features</span>
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<h1>Sequence and Features</h1>
 
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<h1>References</h1>
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        1. Ong, E., Gilkes, N. R., Miller, R. C., Warren, R. A. & Kilburn, D. G. Te
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cellulose-binding domain (CBD(Cex)) of an exoglucanase from Cellulomonas
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fmi: production in Escherichia coli and characterization of the polypeptide.
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Biotechnol. Bioeng. 42, 401–409 (1993). <br>
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<br>
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2. 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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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K5143007 parameters</partinfo>
 
<partinfo>BBa_K5143007 parameters</partinfo>
 
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Latest revision as of 13:34, 1 October 2024

ScCBD_cex'V1 : a Cellulose Binding Domain that enables the fixation of proteins to Cellulose


Protein Description

Description

ScCBD_cex'V1 (Cellulose Binding Domain) is a peptide that has a huge affinity for bacterial cellulose. When fused with another protein, ScCBD_cex'V1 enables the fixation of the protein on the bacterial cellulose.

CBD_CexV1
Figure 1: ScCBD_Cex'V1 three-dimensional structure
Functional cellulose
Figure 2: Functional cellulose
ScCBD_Cex coding sequence
Figure 3: ScCBD_Cex coding sequence

Construction

ScCBD-Cex'V1 was synthesised and its nucleotide sequence optimised for synthesis and expression in Saccharomyces cerevisiae. ScCDB-Cex'V1 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

1. 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).

2. 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.