Difference between revisions of "Part:BBa K3468027"
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<partinfo>BBa_K3468027 short</partinfo>
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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 A40P,S54W,A80V,T113P,T116R,Q119D,Q127L,S193R,S214F,K252L,T266P,N275F position which can be more stable in higher temperature compared with the wild type.
 
  
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<!-- The benzene ring is located in a gully between two aromatic residues TYR87 and TRP185.
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The distance of PI-PI bond is 4.7A between TRP185 and the benzene ring in part of the first MHET.
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The whole ligand just fits into the pocket and binds tightly.
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Three residues of Ser160, Asp206 and His237 formed a catalytic triplet, and ranging was performed: Y87:4.7A ;M161:5.1A; H237:4.7A.
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Significance of molecular docking for mutant work:
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The molecular docking model can predict the binding mode and affinity of mutants and ligands, and promote the work of mutants by analyzing the result model.
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===Usage and Biology===
 
===Usage and Biology===
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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.
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K3468027 SequenceAndFeatures</partinfo>
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<partinfo>BBa_K3468068 SequenceAndFeatures</partinfo>
  
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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.
  
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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.
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[[File:PETase A40P,S54W,A80V,T113P,T116R,Q119D,Q127L,S193R,S214F,K252L,T266P,N275F.jpeg|400px|thumb|left|Fig.1 PETase A40P,S54W,A80V,T113P,T116R,Q119D,Q127L,S193R,S214F,K252L,T266P,N275F in docking]]
 
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===Functional Parameters===
 
===Functional Parameters===
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<partinfo>BBa_K3468027 parameters</partinfo>
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<partinfo>BBa_K3468068 parameters</partinfo>
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Revision as of 15:12, 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,A80V,T113P,T116R,Q119D,Q127L,S193R,S214F,K252L,T266P,N275F in docking