Difference between revisions of "Part:BBa K3187019"

 
Line 3: Line 3:
 
<partinfo>BBa_K3187019 short</partinfo>
 
<partinfo>BBa_K3187019 short</partinfo>
  
−
Lorem ipsum dolor sit amet, consetetur sadipscing elitr, sed diam nonumy eirmod tempor invidunt ut labore et dolore magna aliquyam erat, sed diam voluptua. At vero eos et accusam et justo duo dolores et ea rebum. Stet clita kasd gubergren, no sea takimata sanctus est Lorem ipsum dolor sit amet. Lorem ipsum dolor sit amet, consetetur sadipscing elitr, sed diam nonumy eirmod tempor invidunt ut labore et dolore magna aliquyam erat, sed diam voluptua. At vero eos et accusam et justo duo dolores et ea rebum. Stet clita kasd gubergren, no sea takimata sanctus est Lorem ipsum dolor sit amet.
+
<html>
 +
<h3>Profile</h3>
 +
<table style=“width:80%“>
 +
<tr>
 +
<td><b>Name</b></td>
 +
<td>LPETGG</td>
 +
</tr>
 +
<tr>
 +
<td><b>Base pairs</b></td>
 +
<td>18</td>
 +
</tr>
 +
<tr>
 +
<td><b>Molecular weight</b></td>
 +
<td>1.478 kDa</td>
 +
</tr>
 +
<tr>
 +
<td><b>Origin</b></td>
 +
<td>Synthetic</td>
 +
</tr>
 +
<tr>
 +
<td><b>Part</b></td>
 +
<td>Basic part</td>
 +
</tr>
 +
<tr>
 +
<td><b>Properties</b></td>
 +
<td>Recognition sequence for sortase A </td>
 +
</tr>
 +
</table>
  
 +
<h3>Usage and biology</h3>
 +
<p>Generally, the amino acid sequence LPXTG (X can be any amino acid) is a recognition sequence for the Sortase A.
 +
  It is found in <i>S. aureus</i> and  is  important for anchoring exoproteins in the peptidoglycan layer.
 +
  Exoproteins are pathogenicity. LPXTG is recognized by sortase A a transpeptidase which cleaves between the threonine
 +
  and the glycine. The threonine forms an amid bond with the pentaglycine sequence of the peptidoglycan layer. As a result, a
 +
  covalently bond is produced. It  has been proven  that the sequence LPETG is well recognized by sortase A
 +
    <sup id="cite_ref-1" class="reference">
 +
            <a href="#cite_note-1">[1] </a>
 +
          </sup>.
 +
    LPXTG is an easy opportunity to modify proteins, for example with peptides or other proteins that contains a polyG tag.
 +
    We used a tag with four glycines <a href="https://parts.igem.org/Part:BBa_K3187018"target="_blank">BBa_K3187018</a>.
 +
    Thus VLPs are easily modified since they are made of proteins.
 +
    <br>LPETGG is also possible recognized by sortase A. We used this sequence, since it was used in the publication,
 +
    we based our project on.
 +
    <sup id="cite_ref-2" class="reference">
 +
        <a href="#cite_note-2">[2] </a>
 +
    </sup>
 +
    <br>LPETGG consists of six amino acids (lysine, proline, glutamine acid, threonine and two glycines)  The molecular weight
 +
    is 1.478 kDa.
 +
</p>
 +
<h2>References</h2>
 +
<ol class="references">
 +
  <li id="cite_note-1">
 +
    <span class="mw-cite-backlink">
 +
      <a href="#cite_ref-1">↑</a>
 +
    </span>
 +
    <span class="reference-text">
 +
            Silvie Hansenová Maňásková , Kamran Nazmi, Alex van Belkum, Floris J. Bikker, Willem J. B. van Wamel, Enno C. I. Veerman,
 +
            Synthetic LPETG-Containing Peptide Incorporation in the <i>Staphylococcus aureus</i> Cell-Wall in a Sortase A- and Growth
 +
            Phase-Dependent Manner, plos one, 19.02.2014
 +
    <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1371/journal.pone.0089260 ">[1] </a>
 +
    </span>
 +
  </li>
 +
 +
    <li id="cite_note-2">
 +
          <span class="mw-cite-backlink">
 +
            <a href="#cite_ref-2">↑</a>
 +
          </span>
 +
          <span class="reference-text">
 +
                Dustin Patterson,*,†Benjamin Schwarz,‡John Avera,‡Brian Western,†Matthew Hicks,†Paul Krugler,†Matthew Terra,
 +
                †Masaki Uchida,‡Kimberly McCoy,‡and Trevor Douglas*,Sortase-Mediated Ligation as a Modular Approach for the
 +
                Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22Virus-like Particle, Bioconjugate
 +
                Chemistry, 2017, 28, 2114−2124
 +
          <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1371/journal.pone.0089260 ">[2] </a>
 +
          </span>
 +
        </li>
 +
</ol>
 +
</html>
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===

Revision as of 06:49, 16 October 2019


LPETGG Tag for Sortase-mediated Ligation

Profile

Name LPETGG
Base pairs 18
Molecular weight 1.478 kDa
Origin Synthetic
Part Basic part
Properties Recognition sequence for sortase A

Usage and biology

Generally, the amino acid sequence LPXTG (X can be any amino acid) is a recognition sequence for the Sortase A. It is found in S. aureus and is important for anchoring exoproteins in the peptidoglycan layer. Exoproteins are pathogenicity. LPXTG is recognized by sortase A a transpeptidase which cleaves between the threonine and the glycine. The threonine forms an amid bond with the pentaglycine sequence of the peptidoglycan layer. As a result, a covalently bond is produced. It has been proven that the sequence LPETG is well recognized by sortase A [1] . LPXTG is an easy opportunity to modify proteins, for example with peptides or other proteins that contains a polyG tag. We used a tag with four glycines BBa_K3187018. Thus VLPs are easily modified since they are made of proteins.
LPETGG is also possible recognized by sortase A. We used this sequence, since it was used in the publication, we based our project on. [2]
LPETGG consists of six amino acids (lysine, proline, glutamine acid, threonine and two glycines) The molecular weight is 1.478 kDa.

References

  1. ↑ Silvie Hansenová Maňásková , Kamran Nazmi, Alex van Belkum, Floris J. Bikker, Willem J. B. van Wamel, Enno C. I. Veerman, Synthetic LPETG-Containing Peptide Incorporation in the Staphylococcus aureus Cell-Wall in a Sortase A- and Growth Phase-Dependent Manner, plos one, 19.02.2014 [1]
  2. ↑ Dustin Patterson,*,†Benjamin Schwarz,‡John Avera,‡Brian Western,†Matthew Hicks,†Paul Krugler,†Matthew Terra, †Masaki Uchida,‡Kimberly McCoy,‡and Trevor Douglas*,Sortase-Mediated Ligation as a Modular Approach for the Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22Virus-like Particle, Bioconjugate Chemistry, 2017, 28, 2114−2124 [2]
Sequence and Features


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]