Assessment of the PETase conformational changes induced bypoly(ethylene terephthalate) binding
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Other documents of the author: Costa, Clauber Henrique Souza da; dos Santos, lberto M.; Nahum Alves, Cláudio; Martí, Sergio; Moliner, Vicent; Santana, Kauê; Lameira, Jerônimo
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https://doi.org/10.1002/prot.26155 |
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Title
Assessment of the PETase conformational changes induced bypoly(ethylene terephthalate) bindingAuthor (s)
Date
2021-06-02Publisher
Wiley; Wiley-LissISSN
0887-3585; 1097-0134Bibliographic citation
da Costa, CHS, dos Santos, AM, Alves, CN, et al. Assessment of the PETase conformational changes induced by poly(ethylene terephthalate) binding. Proteins. 2021; 89( 10): 1340– 1352. https://doi.org/10.1002/prot.26155Type
info:eu-repo/semantics/articleVersion
info:eu-repo/semantics/publishedVersionSubject
Abstract
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 (IsPETase) catalyzes the ... [+]
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 (IsPETase) 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 IsPETase 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 interactions of PET in the active site of IsPETase remain unclear. Herein, molecular docking and molecular dynamics (MD) simulations were applied to analyze structural changes of IsPETase induced by PET binding. Results from the essential dynamics revealed that the β1-β2 connecting loop is very flexible. This loop is located far from the active site of IsPETase and we suggest that it can be considered for mutagenesis to increase the thermal stability of IsPETase. The free energy landscape (FEL) demonstrates that the main change in the transition between the unbound to the bound state is associated with the 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 IsPETase 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 plastic polymers using biological systems. [-]
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Proteins.2021;89:1340–1352.Funder Name
Conselho Nacional de Desenvolvimento Científico e Tecnológico | Coordenação deAperfeiçoamento de Pessoal de Nível Superior | Generalitat Valenciana | Ministerio de Ciencia e Innovación | Universitat Jaume I
Project code
306014/2018-1 | 308254/2017-1 | 402572/2018-1 | 88882.466102/2019-01 | 88887.599350/2021-00 | AICO/2019/195 | PGC2018-094852-B-C21 | UJI-B2020-03
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© 2021 Wiley Periodicals LLC
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