Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum.,Wu B, Yee A, Pineda-Lucena A, Semesi A, Ramelot TA, Cort JR, Jung JW, Edwards A, Lee W, Kennedy M, Arrowsmith CH Protein Sci. 2003 Dec;12(12):2831-7. PMID:14627743[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu B, Yee A, Pineda-Lucena A, Semesi A, Ramelot TA, Cort JR, Jung JW, Edwards A, Lee W, Kennedy M, Arrowsmith CH. Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum. Protein Sci. 2003 Dec;12(12):2831-7. PMID:14627743
