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Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7
Psychrophilic enzymes evolved from a plethora of structural scaffolds via multiple molecular pathways. Elucidating their adaptive strategies is instrumental to understand how life can thrive in cold ecosystems and to tailor enzymes for biotechnological applications at low temperatures. In this work,...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4815018/ https://www.ncbi.nlm.nih.gov/pubmed/27029646 http://dx.doi.org/10.1038/srep23776 |
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author | Zanphorlin, Leticia Maria de Giuseppe, Priscila Oliveira Honorato, Rodrigo Vargas Tonoli, Celisa Caldana Costa Fattori, Juliana Crespim, Elaine de Oliveira, Paulo Sergio Lopes Ruller, Roberto Murakami, Mario Tyago |
author_facet | Zanphorlin, Leticia Maria de Giuseppe, Priscila Oliveira Honorato, Rodrigo Vargas Tonoli, Celisa Caldana Costa Fattori, Juliana Crespim, Elaine de Oliveira, Paulo Sergio Lopes Ruller, Roberto Murakami, Mario Tyago |
author_sort | Zanphorlin, Leticia Maria |
collection | PubMed |
description | Psychrophilic enzymes evolved from a plethora of structural scaffolds via multiple molecular pathways. Elucidating their adaptive strategies is instrumental to understand how life can thrive in cold ecosystems and to tailor enzymes for biotechnological applications at low temperatures. In this work, we used X-ray crystallography, in solution studies and molecular dynamics simulations to reveal the structural basis for cold adaptation of the GH1 β-glucosidase from Exiguobacterium antarcticum B7. We discovered that the selective pressure of low temperatures favored mutations that redesigned the protein surface, reduced the number of salt bridges, exposed more hydrophobic regions to the solvent and gave rise to a tetrameric arrangement not found in mesophilic and thermophilic homologues. As a result, some solvent-exposed regions became more flexible in the cold-adapted tetramer, likely contributing to enhance enzymatic activity at cold environments. The tetramer stabilizes the native conformation of the enzyme, leading to a 10-fold higher activity compared to the disassembled monomers. According to phylogenetic analysis, diverse adaptive strategies to cold environments emerged in the GH1 family, being tetramerization an alternative, not a rule. These findings reveal a novel strategy for enzyme cold adaptation and provide a framework for the semi-rational engineering of β-glucosidases aiming at cold industrial processes. |
format | Online Article Text |
id | pubmed-4815018 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48150182016-04-04 Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7 Zanphorlin, Leticia Maria de Giuseppe, Priscila Oliveira Honorato, Rodrigo Vargas Tonoli, Celisa Caldana Costa Fattori, Juliana Crespim, Elaine de Oliveira, Paulo Sergio Lopes Ruller, Roberto Murakami, Mario Tyago Sci Rep Article Psychrophilic enzymes evolved from a plethora of structural scaffolds via multiple molecular pathways. Elucidating their adaptive strategies is instrumental to understand how life can thrive in cold ecosystems and to tailor enzymes for biotechnological applications at low temperatures. In this work, we used X-ray crystallography, in solution studies and molecular dynamics simulations to reveal the structural basis for cold adaptation of the GH1 β-glucosidase from Exiguobacterium antarcticum B7. We discovered that the selective pressure of low temperatures favored mutations that redesigned the protein surface, reduced the number of salt bridges, exposed more hydrophobic regions to the solvent and gave rise to a tetrameric arrangement not found in mesophilic and thermophilic homologues. As a result, some solvent-exposed regions became more flexible in the cold-adapted tetramer, likely contributing to enhance enzymatic activity at cold environments. The tetramer stabilizes the native conformation of the enzyme, leading to a 10-fold higher activity compared to the disassembled monomers. According to phylogenetic analysis, diverse adaptive strategies to cold environments emerged in the GH1 family, being tetramerization an alternative, not a rule. These findings reveal a novel strategy for enzyme cold adaptation and provide a framework for the semi-rational engineering of β-glucosidases aiming at cold industrial processes. Nature Publishing Group 2016-03-31 /pmc/articles/PMC4815018/ /pubmed/27029646 http://dx.doi.org/10.1038/srep23776 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Zanphorlin, Leticia Maria de Giuseppe, Priscila Oliveira Honorato, Rodrigo Vargas Tonoli, Celisa Caldana Costa Fattori, Juliana Crespim, Elaine de Oliveira, Paulo Sergio Lopes Ruller, Roberto Murakami, Mario Tyago Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7 |
title | Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7 |
title_full | Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7 |
title_fullStr | Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7 |
title_full_unstemmed | Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7 |
title_short | Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7 |
title_sort | oligomerization as a strategy for cold adaptation: structure and dynamics of the gh1 β-glucosidase from exiguobacterium antarcticum b7 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4815018/ https://www.ncbi.nlm.nih.gov/pubmed/27029646 http://dx.doi.org/10.1038/srep23776 |
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