Assessment of the PETase conformational changes induced bypoly(ethylene terephthalate) binding
Impacto
Scholar |
Otros documentos de la autoría: Costa, Clauber Henrique Souza da; dos Santos, lberto M.; Nahum Alves, Cláudio; Martí, Sergio; Moliner, Vicent; Santana, Kauê; Lameira, Jerônimo
Metadatos
Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/160292
comunitat-uji-handle3:10234/160293
comunitat-uji-handle4:
INVESTIGACIONEste recurso está restringido
https://doi.org/10.1002/prot.26155 |
Metadatos
Título
Assessment of the PETase conformational changes induced bypoly(ethylene terephthalate) bindingAutoría
Fecha de publicación
2021-06-02Editor
Wiley; Wiley-LissISSN
0887-3585; 1097-0134Cita bibliográfica
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.26155Tipo de documento
info:eu-repo/semantics/articleVersión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
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. [-]
Publicado en
Proteins.2021;89:1340–1352.Datos relacionados
Additional supporting information may be found online in theSupporting Information section at the end of this article.Entidad financiadora
Conselho Nacional de Desenvolvimento Científico e Tecnológico | Coordenação deAperfeiçoamento de Pessoal de Nível Superior | Generalitat Valenciana | Ministerio de Ciencia e Innovación | Universitat Jaume I
Código del proyecto o subvención
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
Derechos de acceso
© 2021 Wiley Periodicals LLC
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/restrictedAccess
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/restrictedAccess
Aparece en las colecciones
- INAM_Articles [509]