ArticleScientific reports2016
Oligomerization as a strategy for cold adaptation: Structure and dynamics of the GH1 β-glucosidase from Exiguobacterium antarcticum B7.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 67 citations in OpenAlex.
- Discovery of a cryptic aminoacidic triad involved in the temperature adaptation of GH1 enzymes.The FEBS journal · 2026Article
- Engineering a Cold-Active Cellulase Complex with a Novel Mushroom Cellobiohydrolase for Efficient Biomass Saccharification and Juice Flavor Optimization.Journal of fungi (Basel, Switzerland) · 2026Article
- Quaternary stabilization of a GH2 β-galactosidase from the psychrophile A. ikkensis, a flexible and unstable dimeric enzyme.Protein science : a publication of the Protein Society · 2025Article
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- The Activation Parameters of a Cold-Adapted Short Chain Dehydrogenase Are Insensitive to Enzyme Oligomerization.Biochemistry · 2022Article
- Study on the Biochemical Characterization and Selectivity of Three β-Glucosidases FromFrontiers in microbiology · 2022Article
- Enzymatic Activity and Physicochemical Properties of Soil Profiles of Luvisols.Materials (Basel, Switzerland) · 2021Article
- Industrial applications of cold-adapted enzymes: challenges, innovations and future perspective.3 Biotech · 2021Review
- Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.Marine drugs · 2021Review
- Homodimerization of a glycoside hydrolase family GH1 β-glucosidase suggests distinct activity of enzyme different states.Protein science : a publication of the Protein Society · 2020Article
- Mapping the Transglycosylation Relevant Sites of Cold-Adapted β-d-Galactosidase fromInternational journal of molecular sciences · 2020Article
- High-throughput quantification of protein structural change reveals potential mechanisms of temperature adaptation in Mytilus mussels.BMC evolutionary biology · 2020Article
- Exploring the Molecular Basis for Substrate Affinity and Structural Stability in Bacterial GH39 β-Xylosidases.Frontiers in bioengineering and biotechnology · 2020Article
- Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability.Scientific reports · 2019Article
- Overexpression and characterization of a novel cold-adapted and salt-tolerant GH1 β-glucosidase from the marine bacterium Alteromonas sp. L82.Journal of microbiology (Seoul, Korea) · 2018Article
- Insight into the cold adaptation and hemicellulose utilization of Cladosporium neopsychrotolerans from genome analysis and biochemical characterization.Scientific reports · 2018Article
- Article
- Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase.BMC biotechnology · 2017Article
- The C-Domain of OleuropeinPlant physiology · 2017Article
- New Heterofunctional Supports Based on Glutaraldehyde-Activation: A Tool for Enzyme Immobilization at Neutral pH.Molecules (Basel, Switzerland) · 2017Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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