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2JD5

Sky1p bound to Npl3p-derived substrate peptide

2JD5 の概要
エントリーDOI10.2210/pdb2jd5/pdb
関連するPDBエントリー1HOW 1Q8Y 1Q8Z 1Q97 1Q99
分子名称SERINE/THREONINE-PROTEIN KINASE SKY1, NUCLEOLAR PROTEIN 3, MAGNESIUM ION, ... (5 entities in total)
機能のキーワードmrna export protein, serine/threonine-protein kinase, kinase, transferase, atp-binding, nucleotide-binding
由来する生物種SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
詳細
細胞内の位置Nucleus, nucleolus : Q01560
タンパク質・核酸の鎖数3
化学式量合計87162.88
構造登録者
Nolen, B.,Lukasiewicz, R.,Adams, J.A.,Huang, D.,Ghosh, G. (登録日: 2007-01-04, 公開日: 2007-02-06, 最終更新日: 2023-12-13)
主引用文献Lukasiewicz, R.,Nolen, B.,Adams, J.A.,Ghosh, G.
The Rgg Domain of Npl3P Recruits Sky1P Through Docking Interactions
J.Mol.Biol., 367:249-, 2007
Cited by
PubMed Abstract: The SR protein kinase in yeast, Sky1p, phosphorylates yeast SR-like protein, Npl3p, at a single serine residue located at its C terminus. We report here the X-ray crystal structure of Sky1p bound to a substrate peptide and ADP. Surprisingly, an Npl3p-derived substrate peptide occupies a groove 20 A away from the kinase active site. In vitro studies support the substrate-docking role of this groove. Mutagenesis and binding studies reveal that multiple degenerate short peptide motifs located within the RGG domain of Npl3p serve as the substrate docking motifs. However, a single docking motif is sufficient for its stable interaction with the kinase. Methylation of the docking motifs abolishes kinase binding and phosphorylation of Npl3p. Remarkably, removal of the docking groove in the kinase or the docking motifs of the substrate does not reduce the overall catalytic efficiency of the phosphorylation reaction in any significant manner. We suggest that docking interaction between Sky1p and Npl3p is essential for substrate recruitment and binding specificity.
PubMed: 17239901
DOI: 10.1016/J.JMB.2006.12.031
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 2jd5
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2024-10-30に公開中

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