NDLI: High-resolution structure of the recombinant sweet-tasting protein thaumatin I.

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High-resolution structure of the recombinant sweet-tasting protein thaumatin I.

Content Provider	Semantic Scholar
Author	Masuda, Tetsuya Ohta, Keisuke Mikami, Bunzo Kitabatake, Naofumi
Copyright Year	2011
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.
File Format	PDF HTM / HTML
DOI	10.1107/S174430911101373X
Alternate Webpage(s)	https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/142313/1/S174430911101373X.pdf
Alternate Webpage(s)	http://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/142313/1/S174430911101373X.pdf
PubMed reference number	21636903
Alternate Webpage(s)	https://doi.org/10.1107/S174430911101373X
Journal	Medline
Volume Number	67
Part	6
Journal	Acta crystallographica. Section F, Structural biology and crystallization communications
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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