Difference between revisions of "Part:BBa K3468019:Design"
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===References===
 
===References===
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[1]Wang J, Yao L. Dissecting C-H∙∙∙π and N-H∙∙∙π Interactions in Two Proteins Using a Combined Experimental and Computational Approach. Sci Rep. 2019 Dec 27;9(1):20149.
 +
 +
[2]Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R. Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis. Chembiochem. 2018 Jul 16;19(14):1471-1475.
 +
 +
[3]Zhang X, Zhang Y, Yang G, Xie Y, Xu L, An J, Cui L, Feng Y. Modulation of the thermostability and substrate specificity of Candida rugosa lipase1 by altering the acyl-binding residue Gly414 at the α-helix-connecting bend. Enzyme Microb Technol. 2016 Jan;82:34-41.
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[4]Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science. 1985 Jul 5;229(4708):23-8.

Latest revision as of 13:01, 27 October 2020


PETase N275F


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]


Design Notes

By observing and comparing the structure of PETase, appropriate mutations were constructed and the forces between the residues were modified. N275F was designed by searching for suitable sites around F284 for mutation.


Source

Ideonalla sakaiensis

References

[1]Wang J, Yao L. Dissecting C-H∙∙∙π and N-H∙∙∙π Interactions in Two Proteins Using a Combined Experimental and Computational Approach. Sci Rep. 2019 Dec 27;9(1):20149.

[2]Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R. Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis. Chembiochem. 2018 Jul 16;19(14):1471-1475.

[3]Zhang X, Zhang Y, Yang G, Xie Y, Xu L, An J, Cui L, Feng Y. Modulation of the thermostability and substrate specificity of Candida rugosa lipase1 by altering the acyl-binding residue Gly414 at the α-helix-connecting bend. Enzyme Microb Technol. 2016 Jan;82:34-41.

[4]Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science. 1985 Jul 5;229(4708):23-8.