Download MendeleyThe solution structure of ribosomal protein S17E from Methanobacterium thermoautotrophicum: a structural homolog of the FF domain.
Wu, B., Yee, A., Huang, Y.J., Ramelot, T.A., Cort, J.R., Semesi, A., Jung, J.W., Lee, W., Montelione, G.T., Kennedy, M.A., Arrowsmith, C.H.(2008) Protein Sci 17: 583-588
- PubMed: 18218711
- DOI: https://doi.org/10.1110/ps.073272208
- Primary Citation of Related Structures:
1RQ6 - PubMed Abstract:
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.
Organizational Affiliation:
Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, Toronto, Ontario M5G 2M9, Canada.
