Difference between revisions of "Part:BBa K3468026"

 
Line 1: Line 1:
 
 
__NOTOC__
 
__NOTOC__
<partinfo>BBa_K3468026 short</partinfo>
+
<partinfo>BBa_K3468068 short</partinfo>
  
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 A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P position which can be more stable in higher temperature compared with the wild type.
 
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===
 +
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 S to 46 at D position which can be more stable in higher temperature compared with the wild type.
 +
  
 
<!-- -->
 
<!-- -->
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
<partinfo>BBa_K3468026 SequenceAndFeatures</partinfo>
+
<partinfo>BBa_K3468068 SequenceAndFeatures</partinfo>
  
 +
This mutation increases the hydrogen bond near S46. The hydrogen bond is an interaction formed by N, O and H in a protein, which can stabilize the structure of the protein and improve thermal stability.
  
 +
We use FoldX to judge the thermal stability of S46D and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable.
 +
[[File:PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P.jpeg|400px|thumb|left|Fig.1 PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P in docking]]
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  
 
===Functional Parameters===
 
===Functional Parameters===
<partinfo>BBa_K3468026 parameters</partinfo>
+
<partinfo>BBa_K3468068 parameters</partinfo>
 
<!-- -->
 
<!-- -->

Revision as of 15:10, 27 October 2020

PETase S46D


Sequence and Features


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]

This mutation increases the hydrogen bond near S46. The hydrogen bond is an interaction formed by N, O and H in a protein, which can stabilize the structure of the protein and improve thermal stability.

We use FoldX to judge the thermal stability of S46D and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable.

Fig.1 PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P in docking