Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum |
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Authors: | Wu Bin Yee Adelinda Pineda-Lucena Antonio Semesi Anthony Ramelot Theresa A Cort John R Jung Jin-Won Edwards Aled Lee Weontae Kennedy Michael Arrowsmith Cheryl H |
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Institution: | Northeast Structural Genomics Consortium, Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada. |
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Abstract: | 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. |
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Keywords: | Heteronuclear NMR Methanobacterium thermoautotrophicum ribosomal protein S28E Northeast Structural Genomics Consortium |
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