Part:BBa_K3468019:Design
PETase N275F
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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.