Someya Tatsuhiko, Nameki Nobukazu, Hosoi Haruko, Suzuki Sakura, Hatanaka Hideki, Fujii Michiko, Terada Takaho, Shirouzu Mikako, Inoue Yorinao, Shibata Takehiko, Kuramitsu Seiki, Yokoyama Shigeyuki, Kawai Gota
Department of Industrial Chemistry, Faculty of Engineering, Chiba Institute of Technology, Chiba 275-0016, Japan.
FEBS Lett. 2003 Jan 30;535(1-3):94-100. doi: 10.1016/s0014-5793(02)03880-2.
Small protein B (SmpB) is required for trans-translation, binding specifically to tmRNA. We show here the solution structure of SmpB from an extremely thermophilic bacterium, Thermus thermophilus HB8, determined by heteronuclear nuclear magnetic resonance methods. The core of the protein consists of an antiparallel beta-barrel twisted up from eight beta-strands, each end of which is capped with the second or third helix, and the first helix is located beside the barrel. Its C-terminal sequence (20 residues), which is rich in basic residues, shows a poorly structured form, as often seen in isolated ribosomal proteins. The results are discussed in relation to the oligonucleotide binding fold.
小蛋白B（SmpB）是反式翻译所必需的，它能特异性结合转运信使核糖核酸（tmRNA）。我们在此展示了嗜热栖热菌HB8（Thermus thermophilus HB8）中小蛋白B的溶液结构，该结构是通过异核核磁共振方法测定的。该蛋白的核心由一个由八条β链扭曲而成的反平行β桶组成，每条链的两端都由第二或第三螺旋封闭，第一螺旋位于桶的旁边。其富含碱性残基的C末端序列（20个残基）呈现出结构不佳的形式，这在分离的核糖体蛋白中很常见。我们结合寡核苷酸结合折叠对结果进行了讨论。
