Difference between revisions of "Part:BBa K2719000"
| Line 9: | Line 9: | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
<b>Tertiary structure of GST</b> | <b>Tertiary structure of GST</b> | ||
| − | <p>The tertiary structure was modeled using Swiss-Model, the results are shown on <i>figure </i></p> | + | <p>The tertiary structure was modeled using Swiss-Model, the results are shown on <i>figure 1.</i></p> |
| − | <img src="http://2018.igem.org/File:T--TecCEM--GST3DStructure.png" alt="GST 3D Structure"> | + | <img src="http://2018.igem.org/File:T--TecCEM--GST3DStructure.png" alt="GST 3D Structure"></img> |
<p><i>Figure 1.</i> GST 3D structure, modelled with Swiss-Model</p> | <p><i>Figure 1.</i> GST 3D structure, modelled with Swiss-Model</p> | ||
Revision as of 18:23, 16 October 2018
GST
Glutathione S-transferase (GST) is a peptide derived from Schistosoma japonicum, in which a target protein may be fused on the N-terminal. This fusion allows the purification of the target protein using glutathione affinity and maximize the presence of the protein in soluble state, rather than on inclusion bodies. In addition, this fusion protein gives stability to the domine of Tenascin V and for this is necessary to use a polyproline linker to maintain the original three dimensional structure of the protein.This tag may be later removed by adding a protease recognition site between GST and the target protein (Harper & Speicher, 2013).
<Add more about the biology of this part here
Usage and Biology
Tertiary structure of GST
The tertiary structure was modeled using Swiss-Model, the results are shown on figure 1.
<img src="http://2018.igem.org/File:T--TecCEM--GST3DStructure.png" alt="GST 3D Structure"></img>
Figure 1. GST 3D structure, modelled with Swiss-Model
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 85