3QTM

Structure of S. pombe nuclear import adaptor Nro1 (Space group P21)

3QTM の概要

• エントリーDOI: 10.2210/pdb3qtm/pdb
• 関連するPDBエントリー: 3QTN
• 分子名称: Uncharacterized protein C4B3.07, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: tetratricopeptide repeat, enhancer of translation termination, translation
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast)
• 細胞内の位置: Cytoplasm: Q9USJ7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80082.38

構造登録者

Rispal, D.,Henri, J.,van Tilbeurgh, H.,Graille, M.,Seraphin, B. (登録日: 2011-02-23, 公開日: 2011-09-21, 最終更新日: 2024-10-30)

主引用文献

Rispal, D.,Henri, J.,van Tilbeurgh, H.,Graille, M.,Seraphin, B.
Structural and functional analysis of Nro1/Ett1: a protein involved in translation termination in S. cerevisiae and in O2-mediated gene control in S. pombe
Rna, 17:1213-1224, 2011

PubMed Abstract: In Saccharomyces cerevisiae, the putative 2-OG-Fe(II) dioxygenase Tpa1 and its partner Ett1 have been shown to impact mRNA decay and translation. Hence, inactivation of these factors was shown to influence stop codon read-though. In addition, Tpa1 represses, by an unknown mechanism, genes regulated by Hap1, a transcription factor involved in the response to levels of heme and O(2). The Schizosaccharomyces pombe orthologs of Tpa1 and Ett1, Ofd1, and its partner Nro1, respectively, have been shown to regulate the stability of the Sre1 transcription factor in response to oxygen levels. To gain insight into the function of Nro1/Ett1, we have solved the crystal structure of the S. pombe Nro1 protein deleted of its 54 N-terminal residues. Nro1 unexpectedly adopts a Tetratrico Peptide Repeat (TPR) fold, a motif often responsible for protein or peptide binding. Two ligands, a sulfate ion and an unknown molecule, interact with a cluster of highly conserved amino acids on the protein surface. Mutation of these residues demonstrates that these ligand binding sites are essential for Ett1 function in S. cerevisiae, as investigated by assaying for efficient translation termination.

PubMed: 21610214
DOI: 10.1261/rna.2697111

実験手法

X-RAY DIFFRACTION (2.15 Å)