The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p
The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p
复制标题
DOI：
10.1038/nsb0298-140
复制
发表时间：
1998-02-01
期刊：
影响因子：
--
通讯作者：
Wlodawer, A
中科院分区：
文献类型：
--
作者：
Lubkowski, J;Hennecke, F;Wlodawer, A
用多波长反常衍射法测定了丝状真菌基因3蛋白的两个N-末端结构域（残基1-217）的结构，并以1.46 A的分辨率进行了精细化。每个结构域由五条或八条β链和一条α螺旋组成。尽管缺少序列同源性，但它们的核心叠加了2埃的均方根偏差。这些结构域参与广泛的相互作用，导致马蹄形，脂肪族氨基酸和苏氨酸内衬内部，描绘了F菌毛可能的结合位点。连接结构域的富含甘氨酸的接头在其他高度有序的结构中是不可见的，并且可以赋予感染过程中所需的结构域之间的灵活性。
The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 Angstrom. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process.