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首页> 外文期刊>Nature >Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein.
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Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein.

机译：酿酒酵母磷脂酰肌醇转移蛋白的晶体结构。

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摘要

The yeast phosphatidylinositol-transfer protein (Sec14) catalyses exchange of phosphatidylinositol and phosphatidylcholine between membrane bilayers in vitro. In vivo, Sec14 activity is essential for vesicle budding from the Golgi complex. Here we report a three-dimensional structure for Sec14 at 2.5 A resolution. Sec14 consists of twelve alpha-helices, six beta-strands, eight 3(10)-helices and has two distinct domains. The carboxy-terminal domain forms a hydrophobic pocket which, in the crystal structure, is occupied by two molecules of n-octyl-beta-D-glucopyranoside and represents the phospholipid-binding domain. This pocket is reinforced by a string motif whose disruption in a sec14 temperature-sensitive mutant results in destabilization of the phospholipid-binding domain. Finally, we have identified an unusual surface helix that may play a critical role in driving Sec14-mediated phospholipid exchange. From this structure, we derive the first molecular clues into how a phosphatidylinositol-transfer protein functions.
机译：酵母磷脂酰肌醇转移蛋白（Sec14）在体外催化双层膜之间的磷脂酰肌醇和磷脂酰胆碱的交换。在体内，Sec14活性对于从高尔基复合体出芽的囊泡至关重要。在这里，我们报告了Sec14在2.5 A分辨率下的三维结构。 Sec14由十二个α-螺旋，六个β-链，八个8（10）-螺旋组成，并具有两个不同的域。羧基末端结构域形成疏水口袋，该疏水口袋在晶体结构中被两个正辛基-β-D-吡喃葡萄糖苷分子占据，并代表磷脂结合域。这个口袋由一个字符串基序加强，该基序在sec14温度敏感性突变体中的破坏导致磷脂结合域的不稳定。最后，我们发现了一个异常的表面螺旋，该螺旋可能在驱动Sec14介导的磷脂交换中起关键作用。从这种结构中，我们得出了磷脂酰肌醇转移蛋白如何发挥功能的第一个分子线索。

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