Part:BBa_K3468064:Design
PETase R260F
- 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. R260F was designed by searching for suitable sites around F261 for mutation.
Source
Ideonalla sakaiensis
References
[1]Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science. 1985 Jul 5;229(4708):23-8.
[2]Chatterjee KS, Tripathi V, Das R. A conserved and buried edge-to-face aromatic interaction in small ubiquitin-like modifier (SUMO) has a role in SUMO stability and function. J Biol Chem. 2019 Apr 26;294(17):6772-6784.
[3]Chrtis C, Jaffe R, Maigret B et al. , 1996. Benzene Dimer: A good model for π-π interactions in proteins a comparison between the benzene and the toluene dimers in the gas phase and in an aqueous solution [J] J. Am. Chem. Soc, 118: 11217-11224.
[4]Weber DS, Warren JJ. A survey of methionine-aromatic interaction geometries in the oxidoreductase class of enzymes: What could Met-aromatic interactions be doing near metal sites? J Inorg Biochem. 2018 Sep;186:34-41.