ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
High-resolution structure of the recombinant sweet-tasting protein thaumatin I.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Magnetic effects of thaumatin crystals; observation of crystal growth by magneto-Archimedes levitation and magnetic orientation.PloS one · 2025Article
- New Insight Into the Structure-Activity Relationship of Sweet-Tasting Proteins: Protein Sector and Its Role for Sweet Properties.Frontiers in nutrition · 2021Article
- Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.Frontiers in molecular biosciences · 2018Article
- Hydroxyethyl cellulose matrix applied to serial crystallography.Scientific reports · 2017Article
- A Hypersweet Protein: Removal of The Specific Negative Charge at Asp21 Enhances Thaumatin Sweetness.Scientific reports · 2016Article
- Grease matrix as a versatile carrier of proteins for serial crystallography.Nature methods · 2015Article
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Authors and funding
4 authors.
Funding
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Abstract
Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at a concentration of 50 nM. The crystal structure of a recombinant form of thaumatin I produced in the yeast Pichia pastoris has been determined to a resolution of 1.1 Å. The model was refined with anisotropic B parameters and riding H atoms. A comparison of the diffraction data and refinement statistics for recombinant thaumatin I with those for plant thaumatin I revealed no significant differences in the diffraction data. The R values for recombinant thaumatin I and plant thaumatin I (F(o) > 4σ) were 9.11% and 9.91%, respectively, indicating the final model to be of good quality. Notably, the electron-density maps around Asn46 and Ser63, which differ between thaumatin variants, were significantly improved. Furthermore, a number of H atoms became visible in an OMIT map and could be assigned. The high-quality structure of recombinant thaumatin with H atoms should provide details about sweetness determinants in thaumatin and provide valuable insights into the mechanism of its interaction with taste receptors.
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