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Assessment of the PETase Conformational Changes Induced by Poly(ethylene terephthalate) Binding
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  • Clauber Henrique Costa,
  • Alberto dos Santos,
  • Cláudio Nahum Alves,
  • Sérgio Martí,
  • Vicente Moliner,
  • Kaue Santana,
  • Jeronimo Lameira Silva
Clauber Henrique Costa
Universidade Federal do Pará

Corresponding Author:[email protected]

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Alberto dos Santos
Universidade Federal do Maranhão
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Cláudio Nahum Alves
Universidade Federal do Pará
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Sérgio Martí
Universitat Jaume I
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Vicente Moliner
Universitat Jaume I
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Kaue Santana
Universidade Federal do Oeste do Pará
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Jeronimo Lameira Silva
Universidade Federal do Pará
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Recently, a bacterium strain of Ideonella sakaiensis was identified with the uncommon ability to degrade the poly(ethylene terephthalate) (PET). The PETase from I. sakaiensis strain 201-F6 catalyzes the hydrolysis of PET converting it to mono(2-hydroxyethyl) terephthalic acid (MHET), bis(2-hydroxyethyl)-TPA (BHET), and terephthalic acid (TPA). Despite the potential of this enzyme for mitigation or elimination of environmental contaminants, one of the limitations of the use of PETase for PET degradation is the fact that it acts only at moderate temperature due to its low thermal stability. Besides, molecular details of the main interaction of PET in the active site of PETase remains unclear. Herein, molecular docking and molecular dynamics (MD) simulations were applied to analyze structural changes of PETase induced by PET binding. Results from the essential dynamics revealed that β1-β2 connecting loop is very flexible. This Loop is located far from the active site of PETase and we suggest that it can be considered for mutagenesis in order to increase the thermal stability of PETase. The free energy landscape (FEL) demonstrates that the main change in the transition between the unbounded to the bounded state is associated with β7-α5 connecting loop, where the catalytic residue Asp206 is located. Overall, the present study provides insights into the molecular binding mechanism of PET into the PETase structure and a computational strategy for mapping flexible regions of this enzyme, which can be useful for the engineering of more efficient enzymes for recycling the plastic polymers using biological systems.
02 Mar 2021Submitted to PROTEINS: Structure, Function, and Bioinformatics
03 Mar 2021Submission Checks Completed
03 Mar 2021Assigned to Editor
09 Mar 2021Reviewer(s) Assigned
01 Apr 2021Review(s) Completed, Editorial Evaluation Pending
02 Apr 2021Editorial Decision: Revise Major
28 Apr 20211st Revision Received
29 Apr 2021Assigned to Editor
29 Apr 2021Submission Checks Completed
29 Apr 2021Reviewer(s) Assigned
06 May 2021Review(s) Completed, Editorial Evaluation Pending
06 May 2021Editorial Decision: Revise Minor
13 May 20212nd Revision Received
14 May 2021Submission Checks Completed
14 May 2021Assigned to Editor
23 May 2021Reviewer(s) Assigned
24 May 2021Review(s) Completed, Editorial Evaluation Pending
29 May 2021Editorial Decision: Accept