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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana
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The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana

机译：brazzein的结构,一个甜的蛋白质从野生植物Pentadiplandra非洲brazzeana

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摘要

Brazzein is the smallest sweet-tasting protein and was isolated from the wild African plant Pentadiplandra brazzeana. The brazzein molecule consists of 54 amino-acid residues and four disulfide bonds. Here, the first crystal structure of brazzein is reported at 1.8? resolution and is compared with previously reported solution structures. Despite the overall structural similarity, there are several remarkable differences between the crystal and solution structures both in their backbone folds and side-chain conformations. Firstly, there is an additional -helix in the crystal structure. Secondly, the atomic r.m.s.d.s between the corresponding C-atom pairs are as large as 2.0-2.2? between the crystal and solution structures. Thirdly, the crystal structure exhibits a molecular shape that is similar but not identical to the solution structures. The crystal structure of brazzein reported here will provide additional information and further insights into the intermolecular interaction of brazzein with the sweet-taste receptor.
机译：甜味蛋白和Brazzein是最小的从非洲野生植物被孤立Pentadiplandra brazzeana .由54个氨基酸残基的名二硫键。在1.8结构brazzein报告吗?分辨率和与以前相比报道解决方案结构。结构相似,有几个水晶和之间的显著差异解决方案结构的折叠支柱和侧链构象。一个额外的螺旋晶体结构。其次,原子之间r.m.s.d.s相应的碳原子对是一样大的2.0 - -2.2吗?结构。展品分子形状相似但不相同的解决方案结构。晶体结构的brazzein报道并进一步提供额外的信息洞察分子间的相互作用brazzein用餐前对甜味刺激受体。

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