Sandbox Reserved 1845: Difference between revisions

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== Mutation Sites of Interest ==

To improve the catalytic activity and thermostability of LCC, Tournier et al. (2020) used structure-guided enzyme engineering based on the crystal structure of LCC bound to a model PET substrate. Using [https://en.wikipedia.org/wiki/Docking_(molecular) molecular docking] and enzyme–substrate contact analysis, the researchers identified <scene name='10/1075247/Original_15_mutation_structure/5'>15 Residues</scene> in the first contact shell surrounding the substrate-binding groove. Of these, 11 positions were selected for [https://en.wikipedia.org/wiki/Saturation_mutagenesis#:~:text=Saturation%20mutagenesis%2C%20or%20site%20saturation,amino%20acids%20at%20the%20position. saturation mutagenesis] to determine how mutations could affect PET depolymerization. These sites were chosen for their interactions with the PET-like ligand or their proximity to the active site. Highly conserved residues essential for catalysis or structural stability were excluded. Using [https://consurf.tau.ac.il/consurf_index.php. ConSurf] demonstrates the residues that are conserved over all versions of LCC, to determine what other variations have changed.

To improve the catalytic activity and thermostability of LCC, Tournier et al. (2020) used structure-guided enzyme engineering based on the crystal structure of LCC bound to a model PET substrate. Using [https://en.wikipedia.org/wiki/Docking_(molecular) molecular docking] and enzyme–substrate contact analysis, the researchers identified <scene name='10/1075247/Original_15_mutation_structure/6'>15 Residues</scene> in the first contact shell surrounding the substrate-binding groove. Of these, 11 positions were selected for [https://en.wikipedia.org/wiki/Saturation_mutagenesis#:~:text=Saturation%20mutagenesis%2C%20or%20site%20saturation,amino%20acids%20at%20the%20position. saturation mutagenesis] to determine how mutations could affect PET depolymerization. These sites were chosen for their interactions with the PET-like ligand or their proximity to the active site. Highly conserved residues essential for catalysis or structural stability were excluded. Using [https://consurf.tau.ac.il/consurf_index.php. ConSurf] demonstrates the residues that are conserved over all versions of LCC, to determine what other variations have changed.

[[Image:Conserved amino acids.jpg|400 px|right|thumb|Figure 3: Image of protein structure, amino acids are colored depending on how often they are conserved in structure. Legend is included. ]]

Sandbox Reserved 1845: Difference between revisions

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 == Mutation Sites of Interest ==
-To improve the catalytic activity and thermostability of LCC, Tournier et al. (2020) used structure-guided enzyme engineering based on the crystal structure of LCC bound to a model PET substrate. Using [https://en.wikipedia.org/wiki/Docking_(molecular) molecular docking] and enzyme–substrate contact analysis, the researchers identified <scene name='10/1075247/Original_15_mutation_structure/5'>15 Residues</scene> in the first contact shell surrounding the substrate-binding groove. Of these, 11 positions were selected for [https://en.wikipedia.org/wiki/Saturation_mutagenesis#:~:text=Saturation%20mutagenesis%2C%20or%20site%20saturation,amino%20acids%20at%20the%20position. saturation mutagenesis] to determine how mutations could affect PET depolymerization. These sites were chosen for their interactions with the PET-like ligand or their proximity to the active site. Highly conserved residues essential for catalysis or structural stability were excluded. Using [https://consurf.tau.ac.il/consurf_index.php. ConSurf] demonstrates the residues that are conserved over all versions of LCC, to determine what other variations have changed.
+To improve the catalytic activity and thermostability of LCC, Tournier et al. (2020) used structure-guided enzyme engineering based on the crystal structure of LCC bound to a model PET substrate. Using [https://en.wikipedia.org/wiki/Docking_(molecular) molecular docking] and enzyme–substrate contact analysis, the researchers identified <scene name='10/1075247/Original_15_mutation_structure/6'>15 Residues</scene> in the first contact shell surrounding the substrate-binding groove. Of these, 11 positions were selected for [https://en.wikipedia.org/wiki/Saturation_mutagenesis#:~:text=Saturation%20mutagenesis%2C%20or%20site%20saturation,amino%20acids%20at%20the%20position. saturation mutagenesis] to determine how mutations could affect PET depolymerization. These sites were chosen for their interactions with the PET-like ligand or their proximity to the active site. Highly conserved residues essential for catalysis or structural stability were excluded. Using [https://consurf.tau.ac.il/consurf_index.php. ConSurf] demonstrates the residues that are conserved over all versions of LCC, to determine what other variations have changed.
 [[Image:Conserved amino acids.jpg|400 px|right|thumb|Figure 3: Image of protein structure, amino acids are colored depending on how often they are conserved in structure. Legend is included. ]]