2AYJ
Solution structure of 50S ribosomal protein L40e from Sulfolobus solfataricus
2AYJ の概要
| エントリーDOI | 10.2210/pdb2ayj/pdb |
| 分子名称 | 50S ribosomal protein L40e, ZINC ION (2 entities in total) |
| 機能のキーワード | zn-binding; beta-strand protein, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, translation |
| 由来する生物種 | Sulfolobus solfataricus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 6527.37 |
| 構造登録者 | Wu, B.,Yee, A.,Lukin, J.,Lemak, A.,Semesi, A.,Ramelot, T.,Kennedy, M.,Edward, A.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (登録日: 2005-09-07, 公開日: 2006-08-22, 最終更新日: 2024-05-22) |
| 主引用文献 | Wu, B.,Lukin, J.,Yee, A.,Lemak, A.,Semesi, A.,Ramelot, T.A.,Kennedy, M.A.,Arrowsmith, C.H. Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus Protein Sci., 17:589-596, 2008 Cited by PubMed Abstract: The ribosomal protein L40E from archaeon Sulfolobus solfataricus is a component of the 50S ribosomal subunit. L40E is a 56-residue, highly basic protein that contains a C4 zinc finger motif, CRKC_X(10)_CRRC. Homologs are found in both archaea and eukaryotes but are not present in bacteria. Eukaryotic genomes encode L40E as a ubiquitin-fusion protein. L40E was absent from the crystal structure of euryarchaeota 50S ribosomal subunit. Here we report the three-dimensional solution structure of L40E by NMR spectroscopy. The structure of L40E is a three-stranded beta-sheet with a simple beta2beta1beta3 topology. There are two unique characteristics revealed by the structure. First, a large and ordered beta2-beta3 loop twists to pack across the one side of the protein. L40E contains a buried polar cluster comprising Lys19, Lys20, Cys22, Asn29, and Cys36. Second, the surface of L40E is almost entirely positively charged. Ten conserved basic residues are positioned on the two sides of the surface. It is likely that binding of zinc is essential in stabilizing the tertiary structure of L40E to act as a scaffold to create a broad positively charged surface for RNA and/or protein recognition. PubMed: 18218710DOI: 10.1110/ps.073273008 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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