Starzyk R M, Webster T A, Schimmel P
Science. 1987 Sep 25;237(4822):1614-8. doi: 10.1126/science.3306924.
Previous experimental results along with the structural modeling presented indicate that a nucleotide fold starts in the amino-terminal part of Escherichia coli isoleucyl-transfer RNA synthetase, a single chain polypeptide of 939 amino acids. Internal deletions were created in the region of the nucleotide fold. A set of deletions that collectively span 145 contiguous amino acids yielded active enzymes. Further extensions of the deletions yielded inactive or unstable proteins. The three-dimensional structure of an evidently homologous protein suggests that the active deletions lack portions of a segment that connects two parts of the nucleotide fold. Therefore, the results imply that removal of major sections of the polypeptide that connects these two parts of the fold does not result in major perturbation of the nucleotide binding site.
先前的实验结果以及所呈现的结构模型表明,核苷酸折叠起始于大肠杆菌异亮氨酰 - 转移RNA合成酶的氨基末端部分,该酶是一种由939个氨基酸组成的单链多肽。在核苷酸折叠区域产生了内部缺失。一组总共跨越145个连续氨基酸的缺失产生了活性酶。缺失的进一步延伸产生了无活性或不稳定的蛋白质。一种明显同源蛋白质的三维结构表明,活性缺失部分缺少连接核苷酸折叠两部分的一个片段。因此,结果表明去除连接折叠这两部分的多肽的主要部分不会导致核苷酸结合位点的重大扰动。