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1RQ6

Solution structure of ribosomal protein S17E from Methanobacterium Thermoautotrophicum, Northeast Structural Genomics Consortium Target TT802 / Ontario Center for Structural Proteomics Target Mth0803

Summary for 1RQ6
Entry DOI10.2210/pdb1rq6/pdb
NMR InformationBMRB: 6028
Descriptor30S ribosomal protein S17e (1 entity in total)
Functional Keywordsalpha protein, structural genomics, protein structure initiative, psi, nesg, northeast structural genomics consortium, translation
Biological sourceMethanothermobacter thermautotrophicus
Total number of polymer chains1
Total formula weight7213.34
Authors
Primary citationWu, 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.
The solution structure of ribosomal protein S17E from Methanobacterium thermoautotrophicum: a structural homolog of the FF domain.
Protein Sci., 17:583-588, 2008
Cited by
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.
PubMed: 18218711
DOI: 10.1110/ps.073272208
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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