Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum

Bin Wu, Adelinda Yee, Antonio Pineda-Lucena, Anthony Semesi, Theresa A. Ramelot, John R. Cort, Jin Won Jung, Aled Edwards, Weontae Lee, Michael Kennedy, Cheryl H. Arrowsmith

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


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 β-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 β-barrel and into the flexible C terminus may present a putative binding site for RNA.

Original languageEnglish
Pages (from-to)2831-2837
Number of pages7
JournalProtein Science
Issue number12
Publication statusPublished - 2003 Dec

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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