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 β-barrel twisted up from eight β-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.
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机译：小蛋白 B （SmpB） 是反式翻译所必需的，与 tmRNA 特异性结合。我们在这里展示了通过异核核磁共振方法确定的极嗜热细菌 Thermus thermophilus HB8 的 SmpB 溶液结构。蛋白质的核心由一个由八条β链扭曲起来的反平行β桶组成，其每端都有第二或第三螺旋，第一螺旋位于桶旁边。其 C 末端序列（20 个残基）富含碱性残基，显示出结构不良的形式，这在分离的核糖体蛋白中很常见。本文将讨论结果与寡核苷酸结合折叠的关系。
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