Han Dohyun, Oh Jongkil, Kim Kyunggon, Lim Hyosun, Kim Youngsoo
College of Medicine, Seoul National University, Yongon-Dong, Seoul 110-799, Republic of Korea.
Biochem Biophys Res Commun. 2007 Sep 7;360(4):784-90. doi: 10.1016/j.bbrc.2007.06.129. Epub 2007 Jul 5.
YrrB is a hypothetical protein containing a tetratricopeptide repeat (TPR) domain from a Gram-positive bacterium, Bacillus subtilis. We determined YrrB structure in the C2 space group to 2.5A resolution, which is the first TPR structure of the Gram-positive bacterium B. subtilis. In contrast to other known TPR structures, the concave surface of the YrrB TPR domain is composed of the putative peptide-binding pocket lined with positively-charged residues. This unique charge distribution reveals that YrrB can interact with partner proteins via an unusual TPR-mediated interaction mode, compared to that of other TPR-containing structures. Functional annotation using genomics analysis suggested that YrrB may be an interacting mediator in the complex formation among RNA sulfuration components. No proteins containing a TPR domain have been identified in the biosynthesis of sulfur-containing biomolecules. Thus, YrrB could play a new role as a connecting module among those proteins in the conserved gene cluster for RNA sulfuration.
YrrB是一种来自革兰氏阳性细菌枯草芽孢杆菌的含有四肽重复序列（TPR）结构域的假定蛋白。我们确定了YrrB在C2空间群中的结构，分辨率为2.5埃，这是革兰氏阳性细菌枯草芽孢杆菌的首个TPR结构。与其他已知的TPR结构不同，YrrB TPR结构域的凹面由排列着带正电荷残基的假定肽结合口袋组成。这种独特的电荷分布表明，与其他含TPR的结构相比，YrrB可以通过一种不寻常的TPR介导的相互作用模式与伴侣蛋白相互作用。使用基因组分析进行的功能注释表明，YrrB可能是RNA硫化成分之间复合物形成中的相互作用介质。在含硫生物分子的生物合成中尚未鉴定出含有TPR结构域的蛋白质。因此，YrrB可能作为RNA硫化保守基因簇中那些蛋白质之间的连接模块发挥新的作用。
