ArticleCommunications biology2018
Loss of a conserved salt bridge in bacterial glycosyl hydrolase BgIM-G1 improves substrate binding in temperate environments.
Article in Communications biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Genomic basis of environmental adaptation in the widespread poly-extremophilic Exiguobacterium group.The ISME journal · 2024Article
- Whole genome sequencing and the lignocellulose degradation potential of Bacillus subtilis RLI2019 isolated from the intestine of termites.Biotechnology for biofuels and bioproducts · 2023Article
- Insights into In Vitro Adaptation of EV71 and Analysis of Reduced Virulence by In Silico Predictions.Vaccines · 2023Article
- Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance.Angewandte Chemie (International ed. in English) · 2021Article
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Authors and funding
5 authors.
Funding
Abstract
Salt bridges are the strongest electrostatic interactions in proteins. They substantially contribute to a protein's structural stability. Thus, mutations of salt bridges are typically selected against. Here, we report on the evolutionary loss of a highly conserved salt bridge in the GH1 family glycosyl hydrolase BglM-G1. BglM-G1's gene was found in the bacterial metagenome of a temperate, seasonally cold marine habitat. In BglM-G1, arginine 75 is replaced by a histidine. While fully retaining β-glucosidase activity, BglM-G1 is less heat stable than an H75R variant, in which the salt bridge was artificially re-introduced. However, the
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