|Protein Science (2008) 17:583-8|
|Northeast Structural Genomics Consortium|
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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.
|Models, Molecular Archaeal Proteins Protein Structure, Tertiary Molecular Sequence Data Sequence Alignment Methanobacterium Ribosomal Proteins Protein Folding Binding Sites Amino Acid Sequence Nuclear Magnetic Resonance, Biomolecular Structural Homology, Protein Phosphopeptides Solutions |
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