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1T4O

Crystal structure of rnt1p dsRBD

1T4O の概要
エントリーDOI10.2210/pdb1t4o/pdb
関連するPDBエントリー1T4N
分子名称Ribonuclease III (2 entities in total)
機能のキーワードrnt1p, dsrbd, rna-binding, hydrolase
由来する生物種Saccharomyces cerevisiae (baker's yeast)
タンパク質・核酸の鎖数2
化学式量合計26414.56
構造登録者
主引用文献Leulliot, N.,Quevillon-Cheruel, S.,Graille, M.,Van Tilbeurgh, H.,Leeper, T.C.,Godin, K.S.,Edwards, T.E.,Sigurdsson, S.T.,Rozenkrants, N.,Nagel, R.J.,Ares, M.,Varani, G.
A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III
Embo J., 23:2468-2477, 2004
Cited by
PubMed Abstract: Rnt1 endoribonuclease, the yeast homolog of RNAse III, plays an important role in the maturation of a diverse set of RNAs. The enzymatic activity requires a conserved catalytic domain, while RNA binding requires the double-stranded RNA-binding domain (dsRBD) at the C-terminus of the protein. While bacterial RNAse III enzymes cleave double-stranded RNA, Rnt1p specifically cleaves RNAs that possess short irregular stem-loops containing 12-14 base pairs interrupted by internal loops and bulges and capped by conserved AGNN tetraloops. Consistent with this substrate specificity, the isolated Rnt1p dsRBD and the 30-40 amino acids that follow bind to AGNN-containing stem-loops preferentially in vitro. In order to understand how Rnt1p recognizes its cognate processing sites, we have defined its minimal RNA-binding domain and determined its structure by solution NMR spectroscopy and X-ray crystallography. We observe a new carboxy-terminal helix following a canonical dsRBD structure. Removal of this helix reduces binding to Rnt1p substrates. The results suggest that this helix allows the Rnt1p dsRBD to bind to short RNA stem-loops by modulating the conformation of helix alpha1, a key RNA-recognition element of the dsRBD.
PubMed: 15192703
DOI: 10.1038/sj.emboj.7600260
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 1t4o
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2026-04-22に公開中

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