Assessment of the PETase conformational changes induced bypoly(ethylene terephthalate) binding
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Altres documents de l'autoria: 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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Títol
Assessment of the PETase conformational changes induced bypoly(ethylene terephthalate) bindingAutoria
Data de publicació
2021-06-02Editor
Wiley; Wiley-LissISSN
0887-3585; 1097-0134Cita bibliogràfica
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.26155Tipus de document
info:eu-repo/semantics/articleVersió
info:eu-repo/semantics/publishedVersionParaules clau / Matèries
Resum
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. [-]
Publicat a
Proteins.2021;89:1340–1352.Dades relacionades
Additional supporting information may be found online in theSupporting Information section at the end of this article.Entitat finançadora
Conselho Nacional de Desenvolvimento Científico e Tecnológico | Coordenação deAperfeiçoamento de Pessoal de Nível Superior | Generalitat Valenciana | Ministerio de Ciencia e Innovación | Universitat Jaume I
Codi del projecte o subvenció
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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