Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae
Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae
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DOI：
10.1016/s0014-5793(97)01079-x
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发表时间：
1997-09-15
期刊：
影响因子：
3.5
通讯作者：
Jann, A
中科院分区：
文献类型：
--
作者：
Schmid, D;Pridmore, D;Jann, A
从丁香假单胞菌中分离出一种新的冰成核基因，并在大肠杆菌中过表达为完全活性蛋白，以获得有关冰成核蛋白结构的实验数据，没有发现信号序列或二次糖基化的证据，显示聚集程度的差异可以调节冰成核活性。纯化蛋白质的圆二色光谱表明存在β-折叠结构，这一发现支持了最近提出的冰核蛋白质结构的假设模型，该模型为其聚集趋势提供了合理的解释。 (C) 1997 年欧洲生化学会联合会。
A new ice nucleation gene from Pseudomonas syringae was isolated and overexpressed as a fully active protein in Escherichia coli in order to gain experimental data about the structure of ice nucleation proteins, No evidence of a signal sequence or secondary glycosylation was found, Differences in the extent of aggregation were shown to modulate the ice nucleation activity. The circular dichroism spectrum of the purified protein indicated the presence of beta-sheet structure, This finding supports a recently proposed hypothetical model for the structure of ice nucleation proteins, which provides a plausible explanation for their aggregation tendency. (C) 1997 Federation of European Biochemical Societies.