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• W2805419309 endingPage "962" @default.
• W2805419309 startingPage "952" @default.
• W2805419309 abstract "Thermotoga maritima Arginine Binding Protein (TmArgBP) is a valuable candidate for arginine biosensing in diagnostics. This protein is endowed with unusual structural properties that include an extraordinary thermal/chemical stability, a domain swapped structure that undergoes large tertiary and quaternary structural transition, and the ability to form non-canonical oligomeric species. As the intrinsic stability of TmArgBP allows for extensive protein manipulations, we here dissected its structure in two parts: its main body deprived of the swapping fragment (TmArgBP20-233) and the C-terminal peptide corresponding to the helical swapping element. Both elements have been characterized independently or in combination using a repertoire of biophysical/structural techniques. Present investigations clearly indicate that TmArgBP20-233 represents a better scaffold for arginine sensing compared to the wild-type protein. Moreover, our data demonstrate that the ligand-free and the ligand-bound forms respond very differently to this helix deletion. This drastic perturbation has an important impact on the ligand-bound form of TmArgBP20-233 stability whereas it barely affects its ligand-free state. The crystallographic structures of these forms provide a rationale to this puzzling observation. Indeed, the arginine-bound state is very rigid and virtually unchanged upon protein truncation. On the other hand, the flexible ligand-free TmArgBP20-233 is able to adopt a novel state as a consequence of the helix deletion. Therefore, the flexibility of the ligand-free form endows this state with a remarkable robustness upon severe perturbations. In this scenario, TmArgBP dissection highlights an intriguing connection between destabilizing/stabilizing effects and the overall flexibility that could operate also in other proteins." @default.
• W2805419309 created "2018-06-13" @default.
• W2805419309 creator A5038720075 @default.
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• W2805419309 date "2018-09-01" @default.
• W2805419309 modified "2023-10-16" @default.
• W2805419309 title "Domain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization" @default.
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• W2805419309 doi "https://doi.org/10.1016/j.bbapap.2018.05.016" @default.
• W2805419309 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29860047" @default.
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