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2M3F

NMR structure of Rsa1p238-259 from S. Cerevisiae

2M3F の概要
エントリーDOI10.2210/pdb2m3f/pdb
NMR情報BMRB: 18959
分子名称Ribosome assembly 1 protein (1 entity in total)
機能のキーワードhelix, rna binding protein
由来する生物種Saccharomyces cerevisiae (Baker's yeast)
細胞内の位置Nucleus: Q08932
タンパク質・核酸の鎖数1
化学式量合計2840.32
構造登録者
Quinternet, M.,Manival, X. (登録日: 2013-01-17, 公開日: 2013-11-27, 最終更新日: 2024-05-15)
主引用文献Rothe, B.,Back, R.,Quinternet, M.,Bizarro, J.,Robert, M.C.,Blaud, M.,Romier, C.,Manival, X.,Charpentier, B.,Bertrand, E.,Branlant, C.
Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.
Nucleic Acids Res., 42:2015-2036, 2014
Cited by
PubMed Abstract: The yeast Snu13p protein and its 15.5K human homolog both bind U4 snRNA and box C/D snoRNAs. They also bind the Rsa1p/NUFIP assembly factor, proposed to scaffold immature snoRNPs and to recruit the Hsp90-R2TP chaperone complex. However, the nature of the Snu13p/15.5K-Rsa1p/NUFIP interaction and its exact role in snoRNP assembly remained to be elucidated. By using biophysical, molecular and imaging approaches, here, we identify residues needed for Snu13p/15.5K-Rsa1p/NUFIP interaction. By NMR structure determination and docking approaches, we built a 3D model of the Snup13p-Rsa1p interface, suggesting that residues R249, R246 and K250 in Rsa1p and E72 and D73 in Snu13p form a network of electrostatic interactions shielded from the solvent by hydrophobic residues from both proteins and that residue W253 of Rsa1p is inserted in a hydrophobic cavity of Snu13p. Individual mutations of residues in yeast demonstrate the functional importance of the predicted interactions for both cell growth and snoRNP formation. Using archaeal box C/D sRNP 3D structures as templates, the association of Snu13p with Rsa1p is predicted to be exclusive of interactions in active snoRNPs. Rsa1p and NUFIP may thus prevent premature activity of pre-snoRNPs, and their removal may be a key step for active snoRNP production.
PubMed: 24234454
DOI: 10.1093/nar/gkt1091
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 2m3f
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2026-01-28に公開中

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