Nucleotide sequence of the structural gene for colicin E1 and predicted structure of the protein.
Nucleotide sequence of the structural gene for colicin E1 and predicted structure of the protein.
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大肠菌素 E1 结构基因的核苷酸序列和预测的蛋白质结构。
DOI：
10.1073/pnas.79.9.2827
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发表时间：
1982
影响因子：
11.1
通讯作者：
A. Nakazawa
中科院分区：
文献类型：
--
作者：
M. Yamada;Y. Ebina;T. Miyata;T. Nakazawa;A. Nakazawa
我们已经测定了结肠素E1结构基因的核苷酸序列，它由1,566个碱基对组成。从DNA序列推导出该蛋白质的氨基酸序列(522个残基)，计算出其相对分子质量为57,279。从预测的二级结构分析中，多肽的NH2末端似乎有三个连续的长α-螺旋，跨越40、100和35个氨基酸残基。此外，在COOH末端附近有一个多肽区，它与大肠杆菌外膜脂蛋白的NH2末端信号部分和地衣芽孢杆菌的β-内酰胺酶具有同源性。根据氨基酸序列，大多数同源氨基酸都位于预计会出现α-螺旋或β-折叠的区域。预测的蛋白质结构的这些特征可能与结肠素E1在其抗菌作用中作为离子载体以及在其诱导合成过程中作为输出蛋白的性质相对应。
We have determined the nucleotide sequence of the structural gene for colicin E1, which consists of 1,566 base pairs. The amino acid sequence (522 residues) of the protein was derived from the DNA sequence, and the molecular weight was calculated to be 57,279. From the analysis of the predicted secondary structure, there appear to be three consecutive long alpha-helices in the NH2-terminal half of the polypeptide, spanning 40, 100, and 35 amino acid residues. In addition, there is a polypeptide region near the COOH terminus that shows homology to the NH2-terminal signal portions of outer membrane lipoprotein in Escherichia coli and beta-lactamase in Bacillus licheniformis. Most of the homologous amino acids are located in the region where either alpha-helix or beta-sheet would be expected to occur, as determined from the amino acid sequence. These characteristics of the predicted protein structure might correspond to properties of colicin E1 as an ionophore in its antimicrobial action and also as an exported protein during its induced synthesis.