Difference between revisions of "Part:BBa K5049006"
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In 2016, iGEM Team TJUSLS-China made significant progress in developing PET-degrading enzymes, specifically PETase from <em>Ideonella sakaiensis</em> 201-F6. They anchored PETase to the surface of <em>Pichia pastoris</em> using the GPI-related cell wall protein GCW61. Inspired by their work, we explored whether adding anchor proteins enhances PETase functionality and identified potentially better anchors, such as Pir1 from <em>Saccharomyces cerevisiae</em>. We conducted 3D protein structure modeling to compare wild-type PETase, PETase-GCW61, and PETase-Pir1 in terms of 3D images, ligand binding site residues, active site residues, and stability (free energy). These analyses determined the benefits of using anchor proteins and suggested potential improvements in anchor selection. | In 2016, iGEM Team TJUSLS-China made significant progress in developing PET-degrading enzymes, specifically PETase from <em>Ideonella sakaiensis</em> 201-F6. They anchored PETase to the surface of <em>Pichia pastoris</em> using the GPI-related cell wall protein GCW61. Inspired by their work, we explored whether adding anchor proteins enhances PETase functionality and identified potentially better anchors, such as Pir1 from <em>Saccharomyces cerevisiae</em>. We conducted 3D protein structure modeling to compare wild-type PETase, PETase-GCW61, and PETase-Pir1 in terms of 3D images, ligand binding site residues, active site residues, and stability (free energy). These analyses determined the benefits of using anchor proteins and suggested potential improvements in anchor selection. | ||
Revision as of 07:57, 2 September 2024
PGTH1-Xylanase-GCW61
VECTOR DESIGN
Vector Design
In 2016, iGEM Team TJUSLS-China made significant progress in developing PET-degrading enzymes, specifically PETase from Ideonella sakaiensis 201-F6. They anchored PETase to the surface of Pichia pastoris using the GPI-related cell wall protein GCW61. Inspired by their work, we explored whether adding anchor proteins enhances PETase functionality and identified potentially better anchors, such as Pir1 from Saccharomyces cerevisiae. We conducted 3D protein structure modeling to compare wild-type PETase, PETase-GCW61, and PETase-Pir1 in terms of 3D images, ligand binding site residues, active site residues, and stability (free energy). These analyses determined the benefits of using anchor proteins and suggested potential improvements in anchor selection.