NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
复制标题
膜结合噬菌体 Pf1 外壳蛋白的结构和动力学的 NMR 研究。
DOI：
10.1126/science.1925542
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Opella,SJ
中科院分区：
文献类型：
--
作者：
Shon,KJ;Kim,Y;Colnago,LA;Opella,SJ
丝状噬菌体外壳蛋白在病毒组装过程中经历了显著的结构转变，因为它从跨越磷脂双层的细胞膜环境转移到新挤出的病毒颗粒。核磁共振(核磁共振)研究表明，46个残基PF1外壳蛋白的膜结合形式令人惊讶地复杂，有五个不同的区域。二级结构由跨越双分子层的长疏水螺旋(残基19至42)和平行于双分子层平面的短两亲性螺旋(残基6至13)组成。连接两个螺旋的NH2末端(残基1到5)、COOH末端(残基43到46)和残基14到18是可移动的。通过将膜结合外壳蛋白的结构和动力学与核磁共振和中子衍射测定的病毒形式的结构和动力学进行比较，可以确定组装过程的基本特征。
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles. Nuclear magnetic resonance (NMR) studies show the membrane-bound form of the 46-residue Pf1 coat protein to be surprisingly complex with five distinct regions. The secondary structure consists of a long hydrophobic helix (residues 19 to 42) that spans the bilayer and a short amphipathic helix (residues 6 to 13) parallel to the plane of the bilayer. The NH2-terminus (residues 1 to 5), the COOH-terminus (residues 43 to 46), and residues 14 to 18 connecting the two helices are mobile. By comparing the structure and dynamics of the membrane-bound coat protein with that of the viral form as determined by NMR and neutron diffraction, essential features of assembly process can be identified.