INTERFACIAL ACTIVATION OF THE LIPASE PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
INTERFACIAL ACTIVATION OF THE LIPASE PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
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DOI：
10.1038/362814a0
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发表时间：
1993-04-29
期刊：
影响因子：
64.8
通讯作者：
CAMBILLAU, C
中科院分区：
文献类型：
--
作者：
VANTILBEURGH, H;EGLOFF, MP;CAMBILLAU, C
的三维结构的脂肪酶-前脂肪酶复合物，共结晶与混合胶束的磷脂酰胆碱和胆汁盐，已确定在3埃分辨率的X-射线晶体学。盖子是一个覆盖脂肪酶催化三联体的表面螺旋，它采用了一种完全不同的构象，允许磷脂结合到酶的活性位点上。开放的盖子是活性位点的重要组成部分，并与前脂肪酶相互作用。它们一起形成脂质-水界面结合位点。这种盖子结构的重组引起了活性位点环的第二次剧烈构象变化，这反过来又产生了氧阴离子空穴（诱导拟合）。
The three-dimensional structure of the lipase-procolipase complex, co-crystallized with mixed micelles of phosphatidylcholine and bile salt, has been determined at 3 angstrom resolution by X-ray crystallography. The lid, a surface helix covering the catalytic triad of lipase, adopts a totally different conformation which allows phospholipid to bind to the enzyme's active site. The open lid is an essential component of the active site and interacts with procolipase. Together they form the lipid-water interface binding site. This reorganization of the lid structure provokes a second drastic conformational change in an active site loop, which in its turn creates the oxyanion hole (induced fit).