Andrews S C, Smith J M, Guest J R, Harrison P M
Krebs Institute, Department of Molecular Biology & Biotechnology, University, Sheffield, UK.
Biochem Biophys Res Commun. 1989 Jan 31;158(2):489-96. doi: 10.1016/s0006-291x(89)80075-0.
The complete amino acid sequence of bacterioferritin (cytochrome b1) from Escherichia coli-K12 has been derived from the nucleotide sequence of the cloned gene. It comprises 158 amino acid residues giving an Mr of 18,495. The identity of the gene product was confirmed by an 87 residue N-terminal sequence obtained from the purified protein, but it differs significantly from much of the previously published partial amino acid sequence (1). Secondary structure prediction indicates a high alpha-helical content consistent with a 4-helix-bundle conformation. The fully assembled bacterioferritin molecule comprising 24 identical subunits and 12 haem moieties is a tetracosamer with an Mr of approximately 452,000.
来自大肠杆菌K12的细菌铁蛋白（细胞色素b1）的完整氨基酸序列已从克隆基因的核苷酸序列推导得出。它由158个氨基酸残基组成，分子量为18,495。通过从纯化蛋白获得的87个残基的N端序列证实了基因产物的身份，但它与许多先前发表的部分氨基酸序列有显著差异（1）。二级结构预测表明其α-螺旋含量很高，与四螺旋束构象一致。完全组装的细菌铁蛋白分子由24个相同的亚基和12个血红素部分组成，是一个二十四聚体，分子量约为452,000。
