Detergent structure in tetragonal crystals of OmpF porin.
Detergent structure in tetragonal crystals of OmpF porin.
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OmpF 孔蛋白四方晶体中的去污剂结构。
DOI：
10.1016/s0969-2126(01)00241-6
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发表时间：
1995
期刊：
影响因子：
5.7
通讯作者：
PA Timmins
中科院分区：
文献类型：
--
作者：
E. Pebay‐Peyroula;RM Garavito;JP Rosenbusch;M. Zulauf;PA Timmins
背景：X射线晶体学已经解析了五种孔蛋白的高分辨率结构，其中包括来自大肠杆菌的三聚体OmpF孔蛋白的三角晶型。与三角晶型相反，通常与膜中的脂质接触的蛋白质表面暴露并与四角晶型中的两亲物相互作用。因此，tetraphylocene形式可以用来调查蛋白质洗涤剂interactions.ResultsUsing单晶中子衍射研究和两种不同的洗涤剂（其中之一是氘代在其疏水部分），细节的两亲蛋白质相互作用的揭示。去污剂分子结合到所谓的疏水区，该疏水区围绕OmpF孔蛋白三聚体并且在天然环境中暴露于脂质。疏水区两侧的芳环与非极性和极性部分之间的边界一致的detergers.ConclusionIn的四晶型的OmpF孔蛋白，膜暴露区域是从水溶液中访问。它被一层去污剂分子膜所包裹，这可能模拟了蛋白质与生物膜中脂质的相互作用。在三角形形式中，蛋白质-蛋白质相互作用在疏水区占主导地位。这些可能反映了在生物膜中观察到的三聚体之间的紧密相互作用。
Background:The high-resolution structures of five porins have been solved by X-ray crystallography including the trigonal crystal form of the trimeric OmpF porin fromEscherichia coli.In an accompanying article, the structure of the tetragonal form of OmpF porin is presented. In contrast to the trigonal crystal form, the protein surfaces normally in contact with lipids in the membrane are exposed and interact with amphiphiles in the tetragonal crystal. Thus, the tetragonal form can be used to investigate protein–detergent interactions.ResultsUsing single-crystal neutron diffraction studies and two different detergents (one of them deuterated in its hydrophobic moiety), details of the amphiphile–protein interactions are revealed. Detergent molecules bind to the so-called hydrophobic zone that surrounds the OmpF porin trimer and which is exposed to lipid in the native environment. The aromatic rings on both sides of the hydrophobic zone coincide with the boundary between non-polar and polar moieties of the detergents.ConclusionIn the tetragonal crystal form of OmpF porin, the membrane-exposed area is accessible from the aqueous solution. It is coated by a film of detergent molecules, which presumably mimics the interactions of the protein with lipids in the biological membrane. In the trigonal form, protein–protein interactions predominate in the hydrophobic zone. These may reflect the tight interactions between trimers that are observed in the biological membrane.