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Crystal structure of the sweet-tasting protein thaumatin II at 1.27Å.

Abstract：

:Thaumatin, an intensely sweet-tasting protein, elicits a sweet taste sensation at 50 nM. Here the X-ray crystallographic structure of one of its variants, thaumatin II, was determined at a resolution of 1.27 Å. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the Cα atom of G96 in thaumatin II was observed. Furthermore, the side chain of residue 67 in thaumatin II is highly disordered. Since residue 67 is one of two residues critical to the sweetness of thaumatin, the present results suggested that the critical positive charges at positions 67 and 82 are disordered and the flexibility and fluctuation of these side chains would be suitable for interaction of thaumatin molecules with sweet receptors.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Masuda T,Ohta K,Tani F,Mikami B,Kitabatake N

doi

10.1016/j.bbrc.2011.05.158

subject

Has Abstract

pub_date

2011-07-08 00:00:00

pages

457-60

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)00942-9

journal_volume

410

pub_type

杂志文章

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