ArticleThe Biochemical journal2019
Desolvation of the substrate-binding protein TauA dictates ligand specificity for the alkanesulfonate ABC importer TauABC.
Article in The Biochemical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 9 citations in OpenAlex.
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- Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.Communications chemistry · 2023Article
- Ecophysiology and interactions of a taurine-respiring bacterium in the mouse gut.Nature communications · 2023Article
- Recently evolved combination of unique sulfatase and amidase genes enables bacterial degradation of the wastewater micropollutant acesulfame worldwide.Frontiers in microbiology · 2023Article
- Root microbiome diversity and structure of the Sonoran desert buffelgrass (Pennisetum ciliare L.).PloS one · 2023Article
- Thermal tuning of protein hydration in a hyperthermophilic enzyme.Frontiers in molecular biosciences · 2022Article
- The sulfoquinovosyl glycerol binding protein SmoF binds and accommodates plant sulfolipids.Current research in structural biology · 2022Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Under limiting sulfur availability, bacteria can assimilate sulfur from alkanesulfonates. Bacteria utilize ATP-binding cassette (ABC) transporters to internalise them for further processing to release sulfur. In gram-negative bacteria the TauABC and SsuABC ensure internalization, although, these two systems have common substrates, the former has been characterized as a taurine specific system. TauA and SsuA are substrate-binding proteins (SBPs) that bind and bring the alkanesulfonates to the ABC importer for transport. Here, we have determined the crystal structure of TauA and have characterized its thermodynamic binding parameters by isothermal titration calorimetry in complex with taurine and different alkanesulfonates. Our structures revealed that the coordination of the alkanesulfonates is conserved, with the exception of Asp205 that is absent from SsuA, but the thermodynamic parameters revealed a very high enthalpic penalty cost for binding of the other alkanesulfonates relative to taurine. Our molecular dynamic simulations indicated that the different levels of hydration of the binding site contributed to the selectivity for taurine over the other alkanesulfonates. Such selectivity mechanism is very likely to be employed by other SBPs of ABC transporters.
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Registered trials
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