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2AYJ

Solution structure of 50S ribosomal protein L40e from Sulfolobus solfataricus

2AYJ の概要
エントリーDOI10.2210/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
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: 18218710
DOI: 10.1110/ps.073273008
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2ayj
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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