Difference between revisions of "Part:BBa K4143339"
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<partinfo>BBa_K4143339 short</partinfo> | <partinfo>BBa_K4143339 short</partinfo> | ||
| − | Adding this sequence to the end of a protein serves to target it for sequestration inside the T4GALA encapsulin. This is because each cargo protein in an encapsulin can be identified by the presence of a short C-terminal targeting peptide at its end. [1][2] | + | Adding this sequence to the end of a protein serves to target it for sequestration inside the T4GALA encapsulin (BBa_K4143337). This is because each cargo protein in an encapsulin can be identified by the presence of a short C-terminal targeting peptide at its end. [1][2] |
===Usage and Biology=== | ===Usage and Biology=== | ||
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| + | For our project, we aimed to use the targeting peptide to facilitate the encapsulation of an antimicrobial peptide (AMP) inside an encapsulin. For this reason, we included a TEV protease site at the beginning of the targeting peptide for downstream AMP separation and isolation. The AMP sequence is described under part BBa_K4143336 and the encapsulin is characterized by part BBa_K4143337. To facilitate the encapsulation of our AMP, we attached the targeting peptide to the C-terminal end of the AMP. | ||
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| + | <h4>AlphaFold Structural Characterization of AMP + Targeting Peptide | ||
| + | </h4> | ||
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| + | Because no structural information was available for our AMP + targeting peptide, we generated a tertiary structure using AlphaFold (Figure 1). Here, the targeting peptide is seen in the non-alpha-helical portion of the peptide, indicating it likely does not assume alpha helices or beta sheets for its secondary structure. | ||
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| + | [[File:HBCM2-alphafold.png|500px|thumb|left|Figure 1: AlphaFold structural predictions for AMP HBCM2 + targeting peptide. | ||
| + | ]] | ||
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| + | <br clear="all"> | ||
=== References=== | === References=== | ||
Latest revision as of 19:56, 9 October 2022
TEV Protease + T4GALA Encapsulin Targeting Peptide
Adding this sequence to the end of a protein serves to target it for sequestration inside the T4GALA encapsulin (BBa_K4143337). This is because each cargo protein in an encapsulin can be identified by the presence of a short C-terminal targeting peptide at its end. [1][2]
Usage and Biology
For our project, we aimed to use the targeting peptide to facilitate the encapsulation of an antimicrobial peptide (AMP) inside an encapsulin. For this reason, we included a TEV protease site at the beginning of the targeting peptide for downstream AMP separation and isolation. The AMP sequence is described under part BBa_K4143336 and the encapsulin is characterized by part BBa_K4143337. To facilitate the encapsulation of our AMP, we attached the targeting peptide to the C-terminal end of the AMP.
AlphaFold Structural Characterization of AMP + Targeting Peptide
Because no structural information was available for our AMP + targeting peptide, we generated a tertiary structure using AlphaFold (Figure 1). Here, the targeting peptide is seen in the non-alpha-helical portion of the peptide, indicating it likely does not assume alpha helices or beta sheets for its secondary structure.
References
[1]T. W. Giessen and P. A. Silver, “Widespread distribution of encapsulin nanocompartments reveals functional diversity,” Nature Microbiology, vol. 2, no. 6, p. 17029, Mar. 2017, doi: 10.1038/nmicrobiol.2017.29.
[2]J. A. Jones, A. S. Cristie-David, M. P. Andreas, and T. W. Giessen, “Triggered reversible disassembly of an engineered protein nanocage,” bioRxiv, p. 2021.04.19.440480, Jan. 2021, doi: 10.1101/2021.04.19.440480.
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]