Wu Bin, Yee Adelinda, Huang Yuanpeng J, Ramelot Theresa A, Cort John R, Semesi Anthony, Jung Jin-Won, Lee Weontae, Montelione Gaetano T, Kennedy Michael A, Arrowsmith Cheryl H
Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, Toronto, Ontario M5G 2M9, Canada.
Protein Sci. 2008 Mar;17(3):583-8. doi: 10.1110/ps.073272208. Epub 2008 Jan 24.
The ribosomal protein S17E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. S17E is a 62-residue protein conserved in archaea and eukaryotes and has no counterparts in bacteria. Mammalian S17E is a phosphoprotein component of eukaryotic ribosomes. Archaeal S17E proteins range from 59 to 79 amino acids, and are about half the length of the eukaryotic homologs which have an additional C-terminal region. Here we report the three-dimensional solution structure of S17E. S17E folds into a small three-helix bundle strikingly similar to the FF domain of human HYPA/FBP11, a novel phosphopeptide-binding fold. S17E bears a conserved positively charged surface acting as a robust scaffold for molecular recognition. The structure of M. thermoautotrophicum S17E provides a template for homology modeling of eukaryotic S17E proteins in the family.
嗜热自养甲烷杆菌的核糖体蛋白S17E是30S核糖体亚基的一个组成部分。S17E是一种在古菌和真核生物中保守的由62个残基组成的蛋白质,在细菌中没有对应物。哺乳动物的S17E是真核核糖体的一种磷蛋白成分。古菌的S17E蛋白长度在59至79个氨基酸之间,约为具有额外C端区域的真核同源物长度的一半。在此我们报道了S17E的三维溶液结构。S17E折叠成一个小三螺旋束,与人类HYPA/FBP11的FF结构域惊人地相似,这是一种新型的磷酸肽结合折叠。S17E有一个保守的带正电表面,作为分子识别的强大支架。嗜热自养甲烷杆菌S17E的结构为该家族中真核S17E蛋白的同源建模提供了模板。