1NE3
Solution structure of ribosomal protein S28E from Methanobacterium Thermoautotrophicum. Ontario Centre for Structural Proteomics target MTH0256_1_68; Northeast Structural Genomics Target TT744
Summary for 1NE3
| Entry DOI | 10.2210/pdb1ne3/pdb |
| NMR Information | BMRB: 5620 |
| Descriptor | 30S ribosomal protein S28E (1 entity in total) |
| Functional Keywords | beta protein, structural genomics, ocsp, nesg, protein structure initiative, psi, northeast structural genomics consortium, ribosome |
| Biological source | Methanothermococcus thermolithotrophicus |
| Total number of polymer chains | 1 |
| Total formula weight | 7679.06 |
| Authors | Wu, B.,Pineda-Lucena, A.,Yee, A.,Cort, J.R.,Ramelot, T.A.,Kennedy, M.,Edwards, A.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2002-12-10, release date: 2003-12-23, Last modification date: 2024-05-22) |
| Primary citation | Wu, B.,Yee, A.,Pineda-Lucena, A.,Semesi, A.,Ramelot, T.A.,Cort, J.R.,Jung, J.W.,Edwards, A.,Lee, W.,Kennedy, M.,Arrowsmith, C.H. Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum. Protein Sci., 12:2831-2837, 2003 Cited by PubMed 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. PubMed: 14627743DOI: 10.1110/ps.03358203 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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