Difference between revisions of "Part:BBa K3468026"
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<partinfo>BBa_K3468026 short</partinfo>
 
<partinfo>BBa_K3468026 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 mutant is more stable in higher temperature compared with the wild type.
  
 
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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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<partinfo>BBa_K3468026 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468026 SequenceAndFeatures</partinfo>
  
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The phenyl group of N275F formed a “T-shaped” π-π stacking interaction with the phenyl group of F284.
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Q127L prompts the hydrophobic packing in the protein interior
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The indolyl of S54W formed a offset parallel π-π stacking interaction with the phenolic group of the Y69.
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A80V prompts the hydrophobic packing in the protein interior.
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The substitution of proline for threonline in T113P mutation reduced the conformational entropy of the local loop region
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The substitution of proline for threonline in T266P mutation reduced the conformational entropy of the local loop region
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For the Q119D mutation, the substitution of asparate for glutamine in Q119D , conferred new hydrogen bonds with the aminogroup of Ser121 and Ser122
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The phenyl group of S214F formed a offset parallel π-π stacking interaction with the indolyl of the W185.
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For the T116R mutation, the substitution of arginine for threonine in T116R , conferred new hydrogen bonds with the aminogroup of D118
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For the S193R mutation, the substitution of arginine for serine in S193R , conferred new hydrogen bonds with the carboxyl of A171
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The substitution of proline for alanine in A40P mutation reduced the conformational entropy of the local loop region
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K252L prompts the hydrophobic packing in the protein interior.
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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: Y87:4.5A ;M161:4.9A; H237:4.7A.
  
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[[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]]
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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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[[File:PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P.jpeg|400px]
 
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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K3468026 parameters</partinfo>
 
<partinfo>BBa_K3468026 parameters</partinfo>
 
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Revision as of 16:27, 27 October 2020

PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P The PETase is an enzyme, which can hydrolyze PET and this mutation protein is changed on the basis of the PETase.This mutant is more stable in higher temperature compared with the wild type.

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal EcoRI site found at 240
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal EcoRI site found at 240
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal EcoRI site found at 240
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal EcoRI site found at 240
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal EcoRI site found at 240
  • 1000
    COMPATIBLE WITH RFC[1000]

The phenyl group of N275F formed a “T-shaped” π-π stacking interaction with the phenyl group of F284.

Q127L prompts the hydrophobic packing in the protein interior The indolyl of S54W formed a offset parallel π-π stacking interaction with the phenolic group of the Y69. A80V prompts the hydrophobic packing in the protein interior. The substitution of proline for threonline in T113P mutation reduced the conformational entropy of the local loop region The substitution of proline for threonline in T266P mutation reduced the conformational entropy of the local loop region For the Q119D mutation, the substitution of asparate for glutamine in Q119D , conferred new hydrogen bonds with the aminogroup of Ser121 and Ser122 The phenyl group of S214F formed a offset parallel π-π stacking interaction with the indolyl of the W185. For the T116R mutation, the substitution of arginine for threonine in T116R , conferred new hydrogen bonds with the aminogroup of D118 For the S193R mutation, the substitution of arginine for serine in S193R , conferred new hydrogen bonds with the carboxyl of A171 The substitution of proline for alanine in A40P mutation reduced the conformational entropy of the local loop region K252L prompts the hydrophobic packing in the protein interior.










The benzene ring is located in a gully between two aromatic residues TYR87 and TRP185. The distance of PI-PI bond is 4.7A between TRP185 and the benzene ring in part of the first MHET. The whole ligand just fits into the pocket and binds tightly. Three residues of Ser160, Asp206 and His237 formed a catalytic triplet, and ranging was performed: Y87:4.5A ;M161:4.9A; H237:4.7A.

Significance of molecular docking for mutant work: 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. [[File:PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P.jpeg|400px]