1RQ6
Solution structure of ribosomal protein S17E from Methanobacterium Thermoautotrophicum, Northeast Structural Genomics Consortium Target TT802 / Ontario Center for Structural Proteomics Target Mth0803
1RQ6 の概要
| エントリーDOI | 10.2210/pdb1rq6/pdb |
| NMR情報 | BMRB: 6028 |
| 分子名称 | 30S ribosomal protein S17e (1 entity in total) |
| 機能のキーワード | alpha protein, structural genomics, protein structure initiative, psi, nesg, northeast structural genomics consortium, translation |
| 由来する生物種 | Methanothermobacter thermautotrophicus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 7213.34 |
| 構造登録者 | Wu, B.,Yee, A.,Huang, Y.J.,Ramelot, T.A.,Semesi, A.,Jung, J.W.,Edward, A.,Lee, W.,Kennedy, M.A.,Montelione, G.T.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (登録日: 2003-12-04, 公開日: 2004-12-14, 最終更新日: 2024-05-22) |
| 主引用文献 | Wu, B.,Yee, A.,Huang, Y.J.,Ramelot, T.A.,Cort, J.R.,Semesi, A.,Jung, J.W.,Lee, W.,Montelione, G.T.,Kennedy, M.A.,Arrowsmith, C.H. The solution structure of ribosomal protein S17E from Methanobacterium thermoautotrophicum: a structural homolog of the FF domain. Protein Sci., 17:583-588, 2008 Cited by PubMed Abstract: The ribosomal protein S17E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. S17E is a 62-residue protein conserved in archaea and eukaryotes and has no counterparts in bacteria. Mammalian S17E is a phosphoprotein component of eukaryotic ribosomes. Archaeal S17E proteins range from 59 to 79 amino acids, and are about half the length of the eukaryotic homologs which have an additional C-terminal region. Here we report the three-dimensional solution structure of S17E. S17E folds into a small three-helix bundle strikingly similar to the FF domain of human HYPA/FBP11, a novel phosphopeptide-binding fold. S17E bears a conserved positively charged surface acting as a robust scaffold for molecular recognition. The structure of M. thermoautotrophicum S17E provides a template for homology modeling of eukaryotic S17E proteins in the family. PubMed: 18218711DOI: 10.1110/ps.073272208 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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