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, Weon Tae Lee, Michael Kennedy, Cheryl H. Arrowsmith

Research output: Contribution to journalArticle

15 Citations (Scopus)

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 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
Volume12
Issue number12
DOIs
Publication statusPublished - 2003 Dec 1

Fingerprint

Methanobacterium
Ribosomal Proteins
Archaea
RNA
Ribosome Subunits
Proteins
Sequence Homology
Eukaryota
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Binding Sites
Topology

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Wu, B., Yee, A., Pineda-Lucena, A., Semesi, A., Ramelot, T. A., Cort, J. R., ... Arrowsmith, C. H. (2003). Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum. Protein Science, 12(12), 2831-2837. https://doi.org/10.1110/ps.03358203
Wu, Bin ; Yee, Adelinda ; Pineda-Lucena, Antonio ; Semesi, Anthony ; Ramelot, Theresa A. ; Cort, John R. ; Jung, Jin Won ; Edwards, Aled ; Lee, Weon Tae ; Kennedy, Michael ; Arrowsmith, Cheryl H. / Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum. In: Protein Science. 2003 ; Vol. 12, No. 12. pp. 2831-2837.
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Wu, B, Yee, A, Pineda-Lucena, A, Semesi, A, Ramelot, TA, Cort, JR, Jung, JW, Edwards, A, Lee, WT, Kennedy, M & Arrowsmith, CH 2003, 'Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum', Protein Science, vol. 12, no. 12, pp. 2831-2837. https://doi.org/10.1110/ps.03358203

Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum. / Wu, Bin; Yee, Adelinda; Pineda-Lucena, Antonio; Semesi, Anthony; Ramelot, Theresa A.; Cort, John R.; Jung, Jin Won; Edwards, Aled; Lee, Weon Tae; Kennedy, Michael; Arrowsmith, Cheryl H.

In: Protein Science, Vol. 12, No. 12, 01.12.2003, p. 2831-2837.

Research output: Contribution to journalArticle

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AU - Jung, Jin Won

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AU - Kennedy, Michael

AU - Arrowsmith, Cheryl H.

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N2 - 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.

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Wu B, Yee A, Pineda-Lucena A, Semesi A, Ramelot TA, Cort JR et al. Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum. Protein Science. 2003 Dec 1;12(12):2831-2837. https://doi.org/10.1110/ps.03358203