Difference between revisions of "Part:BBa K3468040"
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<partinfo>BBa_K3468040 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468040 SequenceAndFeatures</partinfo> | ||
Adding hydrogen bonds stabilized α3-β5loop, β2-β3loop and β2sheet | Adding hydrogen bonds stabilized α3-β5loop, β2-β3loop and β2sheet | ||
+ | |||
+ | It was predicted by FoldX that DDG decreased. PyOML was used for visual screening, which formed hydrogen bonds with 78-VAL, 144-Pro and 145-ILE. after mutation to ARG, it formed new hydrogen bonds with 71-PRO and 72-THR, which stabilized α3-β5loop, β2-β3loop and β2sheet, | ||
+ | which was beneficial to improve the thermal stability of PETase | ||
+ | [[File:K148R.png|400px|thumb|left|Fig.1 K148R in PyMOL]] | ||
<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display |
Latest revision as of 13:26, 27 October 2020
PETase K148R
The PETase is an enzyme, which can hydrolyze PET and this mutation protein is changed on the basis of the PETase. This protein is changed from K to R at 148 position which can be more stable in higher temperature compared with the wild type.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Adding hydrogen bonds stabilized α3-β5loop, β2-β3loop and β2sheet
It was predicted by FoldX that DDG decreased. PyOML was used for visual screening, which formed hydrogen bonds with 78-VAL, 144-Pro and 145-ILE. after mutation to ARG, it formed new hydrogen bonds with 71-PRO and 72-THR, which stabilized α3-β5loop, β2-β3loop and β2sheet,
which was beneficial to improve the thermal stability of PETase