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タイトル: | High-resolution structure of the recombinant sweet-tasting protein thaumatin I. |
著者: | Masuda, Tetsuya https://orcid.org/0000-0001-5857-5753 (unconfirmed) Ohta, Keisuke Mikami, Bunzo Kitabatake, Naofumi |
著者名の別形: | 桝田, 哲哉 |
キーワード: | thaumatin sweet-tasting proteins Pichia pastoris H atoms |
発行日: | Jun-2011 |
出版者: | International Union of Crystallography |
誌名: | Acta crystallographica. Section F, Structural biology and crystallization communications |
巻: | 67 |
号: | Part 6 |
開始ページ: | 652 |
終了ページ: | 658 |
抄録: | 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. |
著作権等: | © International Union of Crystallography |
URI: | http://hdl.handle.net/2433/142313 |
DOI(出版社版): | 10.1107/S174430911101373X |
PubMed ID: | 21636903 |
出現コレクション: | 学術雑誌掲載論文等 |
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