|Protein Science (2003) 12(12):2831-7|
|Northeast Structural Genomics Consortium|
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The ribosomal protein S28E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. ...
Sequence homologs of S28E are found only in archaea and eukaryotes. Here we report the three-dimensional solution structure of S28E by NMR spectroscopy. S28E contains a globular region and a long C-terminal tail protruding from the core. The globular region consists of four antiparallel beta-strands that are arranged in a Greek-key topology. Unique features of S28E include an extended loop L2-3 that folds back onto the protein and a 12-residue charged C-terminal tail with no regular secondary structure and greater flexibility relative to the rest of the protein. The structural and surface resemblance to OB-fold family of proteins and the presence of highly conserved basic residues suggest that S28E may bind to RNA. A broad positively charged surface extending over one side of the beta-barrel and into the flexible C terminus may present a putative binding site for RNA.
|chemistry metabolism |
|Models, Molecular Molecular Sequence Data Structure-Activity Relationship Protein Conformation Sequence Alignment Methanobacterium Ribosomal Proteins Protein Folding Amino Acid Sequence Nuclear Magnetic Resonance, Biomolecular Bacterial Proteins |
|15 (Last update: 05/27/2017 11:24:05am)|
|Protein Sci. 2003 Dec;12(12):2831-7.|