FD COAT PROTEIN-STRUCTURE IN MEMBRANE ENVIRONMENTS
FD COAT PROTEIN-STRUCTURE IN MEMBRANE ENVIRONMENTS
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DOI：
10.1006/jmbi.1993.1523
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发表时间：
1993-10-05
影响因子：
5.6
通讯作者：
OPELLA, SJ
中科院分区：
文献类型：
--
作者：
MCDONNELL, PA;SHON, K;OPELLA, SJ
噬菌体fd外壳蛋白的膜结合形式在双层平面上具有长的疏水膜跨越螺旋和较短的两亲螺旋。 N 和 C 末端附近以及依次连接两个螺旋的残基是可移动的。通过结合胶束中蛋白质样品的多维溶液核磁共振实验和定向和非定向脂质双层中蛋白质样品的高分辨率固态核磁共振实验的结果，对螺旋二级结构元件的位置和方向以及蛋白质主链动力学进行了表征。外壳蛋白是胶束中的单体。 fd外壳蛋白的膜结合形式的二级结构与病毒颗粒中发现的结构形式非常相似，因为它几乎都是α螺旋。然而，蛋白质的膜结合形式与病毒颗粒中蛋白质的结构形式在二级结构的排列上不同，因为蛋白质的膜结合形式具有两个彼此垂直定向的不同螺旋结构域，而病毒颗粒中蛋白质的结构形式具有大致沿丝轴排列的近乎连续的螺旋。此外，两个螺旋之间的弯曲处和C末端附近的残基的动力学存在显着差异，因为它们在蛋白质的膜结合形式中是可移动的，而不是在病毒颗粒中。 N 末端的残基 1 至 5 在外壳蛋白的膜结合形式和结构形式中均具有高度可移动性且非结构化。
The membrane bound form of bacteriophage fd coat protein has a long hydrophobic membrane spanning helix and a shorter amphipathic helix in the plane of the bilayer. Residues near the N and C termini and in the turn connecting the two helices are mobile. The locations and orientations of the helical secondary structure elements and the protein backbone dynamics were characterized by combining results from multidimensional solution NMR experiments on protein samples in micelles and high resolution solid-state NMR experiments on protein samples in oriented and unoriented lipid bilayers. The coat protein is a monomer in micelles. The secondary structure of the membrane bound form of fd coat protein is very similar to that of the structural form found in the virus particles, since it is nearly all alpha helix. However, the membrane bound form of the protein differs from the structural form of the protein in virus particles in the arrangement of the secondary structure, since the membrane bound form of the protein has two distinct helical domains oriented perpendicular to each other and the structural form of the protein in the virus particles has a nearly continuous helix aligned approximately along the filament axis. In addition, there are substantial differences in the dynamics of residues in the bend between the two helices and near the C terminus, since they are mobile in the membrane bound form of the protein and not in the virus particles. Residues 1 to 5 at the N terminus are highly mobile and unstructured in both the membrane bound and structural forms of the coat protein.