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Title: High-resolution structure of the recombinant sweet-tasting protein thaumatin I.
Authors: Masuda, Tetsuya  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-5857-5753 (unconfirmed)
Ohta, Keisuke
Mikami, Bunzo  kyouindb  KAKEN_id
Kitabatake, Naofumi
Author's alias: 桝田, 哲哉
Keywords: thaumatin
sweet-tasting proteins
Pichia pastoris
H atoms
Issue Date: Jun-2011
Publisher: International Union of Crystallography
Journal title: Acta crystallographica. Section F, Structural biology and crystallization communications
Volume: 67
Issue: Part 6
Start page: 652
End page: 658
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.
Rights: © International Union of Crystallography
URI: http://hdl.handle.net/2433/142313
DOI(Published Version): 10.1107/S174430911101373X
PubMed ID: 21636903
Appears in Collections:Journal Articles

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