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Assessment of Kaistella jeonii esterase conformational dynamics in response to poly(ethylene terephthalate) binding.
Pinto, Ederson Sales Moreira; Mangini, Arthur Tonietto; Novo, Lorenzo Chaves Costa; Cavatao, Fernando Guimaraes; Krause, Mathias J; Dorn, Marcio.
Afiliación
  • Pinto ESM; Center for Biotechnology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, Buildings 43421, Porto Alegre, RS, Brazil.
  • Mangini AT; Center for Biotechnology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, Buildings 43421, Porto Alegre, RS, Brazil.
  • Novo LCC; Center for Biotechnology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, Buildings 43421, Porto Alegre, RS, Brazil.
  • Cavatao FG; Center for Biotechnology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, Buildings 43421, Porto Alegre, RS, Brazil.
  • Krause MJ; Institute for Applied and Numerical Mathematics, Karlsruhe Institute of Technology, Englerstraße 2, D-76131, Karlsruhe, BW, Germany.
  • Dorn M; Center for Biotechnology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, Buildings 43421, Porto Alegre, RS, Brazil.
Curr Res Struct Biol ; 7: 100130, 2024.
Article en En | MEDLINE | ID: mdl-38406590
ABSTRACT
The pervasive presence of plastic in the environment has reached a concerning scale, being identified in many ecosystems. Bioremediation is the cheapest and most eco-friendly alternative to remove this polymer from affected areas. Recent work described that a novel cold-active esterase enzyme extracted from the bacteria Kaistella jeonii could promiscuously degrade PET. Compared to the well-known PETase from Ideonella sakaiensis, this novel esterase presents a low sequence identity yet has a remarkably similar folding. However, enzymatic assays demonstrated a lower catalytic efficiency. In this work, we employed a strict computational approach to investigate the binding mechanism between the esterase and PET. Understanding the underlying mechanism of binding can shed light on the evolutive mechanism of how enzymes have been evolving to degrade these artificial molecules and help develop rational engineering approaches to improve PETase-like enzymes. Our results indicate that this esterase misses a disulfide bridge, keeping the catalytic residues closer and possibly influencing its catalytic efficiency. Moreover, we describe the structural response to the interaction between enzyme and PET, indicating local and global effects. Our results aid in deepening the knowledge behind the mechanism of biological catalysis of PET degradation and as a base for the engineering of novel PETases.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Curr Res Struct Biol Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Curr Res Struct Biol Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Países Bajos