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首页> 外文期刊>Journal of Structural Biology >STAPHYLOCOCCUS AUREUS ALPHA-TOXIN - CHARACTERIZATION OF PROTEIN/LIPID INTERACTIONS, 2D CRYSTALLIZATION ON LIPID MONOLAYERS, AND 3D STRUCTURE
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STAPHYLOCOCCUS AUREUS ALPHA-TOXIN - CHARACTERIZATION OF PROTEIN/LIPID INTERACTIONS, 2D CRYSTALLIZATION ON LIPID MONOLAYERS, AND 3D STRUCTURE

机译:金黄色葡萄球菌α-毒素-蛋白质/脂质相互作用的表征,脂质单分子层上的二维结晶和3D结构

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Staphylococcus aureus alpha-toxin was characterized with respect to surface activity and its interaction with lipid monolayers. The protein alone had a detergent-like behavior at the air/water interface. Its affinity was higher for negatively charged than for neutral phospholipids. The interaction was pH dependent, showing a maximum increase at pH 7.0. Only a small part of the protein oligomer appeared to be inserted into the monolayers., crystalline sheets of alpha-toxin were formed using negatively charged phospholipids. Electron microscopy of such areas, at different tilt angles, allowed reconstruction of a three-dimensional model following image processing, The sheets analyzed consisted of two protein layers arranged on a tetragonal lattice. Under the conditions used to grow the crystals the toxin formed 90-Angstrom-wide cylinders with a height of 70 Angstrom. One of the imposed fourfold axes running perpendicular to the plane of the crystalline layer is positioned at a protein-deficient region which forms a 25-Angstrom-wide pore. through the oligomer, (C) 1997 Academic Press. [References: 31]
机译:金黄色葡萄球菌α-毒素的表面活性及其与脂质单层的相互作用方面进行了表征。单独的蛋白质在空气/水界面处具有类似洗涤剂的行为。它对带负电的亲和力高于对中性磷脂。相互作用是pH依赖性的,在pH 7.0下显示最大增加。似乎只有一小部分蛋白质寡聚体插入单层中。使用带负电荷的磷脂形成了α-毒素晶体片。在不同的倾斜角度对这些区域进行电子显微镜检查,可以在图像处理后重建三维模型。分析的薄片由排列在四方晶格上的两个蛋白质层组成。在用于生长晶体的条件下,毒素形成了90埃宽的圆柱体,高度为70埃。垂直于结晶层平面延伸的四重轴之一位于蛋白质不足区域,该区域形成25埃宽的孔。通过低聚物,(C)1997 Academic Press。 [参考:31]

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