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首页> 外文期刊>Journal of Molecular Biology >The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme.
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The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme.

机译：枯草芽孢杆菌脂肪酶的晶体结构：最小的α/β水解酶折叠酶。

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摘要

The X-ray structure of the lipase LipA from Bacillus subtilis has been determined at 1.5 A resolution. It is the first structure of a member of homology family 1.4 of bacterial lipases. The lipase shows a compact minimal alpha/beta hydrolase fold with a six-stranded parallel beta-sheet flanked by five alpha-helices, two on one side of the sheet and three on the other side. The catalytic triad residues, Ser77, Asp133 and His156, and the residues forming the oxyanion hole (backbone amide groups of Ile12 and Met78) are in positions very similar to those of other lipases of known structure. However, no lid domain is present and the active-site nucleophile Ser77 is solvent-exposed. A model of substrate binding is proposed on the basis of a comparison with other lipases with a covalently bound tetrahedral intermediate mimic. It explains the preference of the enzyme for substrates with C8 fatty acid chains.
机译：枯草芽孢杆菌的脂肪酶LipA的X射线结构已确定为1.5 A分辨率。它是细菌脂肪酶同源家族1.4的成员的第一个结构。脂肪酶显示紧凑的最小α/β水解酶折叠，带有六链平行的β-折叠，两侧是五个α-螺旋，两个在折叠的一侧，三个在另一侧。催化三联体残基Ser77，Asp133和His156，以及形成氧阴离子孔的残基（Ile12和Met78的骨酰胺基）的位置与已知结构的其他脂肪酶的位置非常相似。然而，不存在盖结构域，并且活性位亲核体Ser77暴露于溶剂中。基于与具有共价结合的四面体中间模拟物的其他脂肪酶的比较，提出了底物结合的模型。它解释了酶对具有C8脂肪酸链的底物的偏爱。

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