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1SI7

Structure of E. coli tRNA psi 13 pseudouridine synthase TruD

1SI7 の概要
エントリーDOI10.2210/pdb1si7/pdb
分子名称tRNA pseudouridine synthase D (2 entities in total)
機能のキーワードtrud, pseudouridine synthase, trna, novel fold, lyase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数1
化学式量合計41311.76
構造登録者
Kaya, Y.,Del Campo, M.,Ofengand, J.,Malhotra, A. (登録日: 2004-02-27, 公開日: 2004-03-16, 最終更新日: 2024-04-03)
主引用文献Kaya, Y.,Del Campo, M.,Ofengand, J.,Malhotra, A.
Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold
J.Biol.Chem., 279:18107-18110, 2004
Cited by
PubMed Abstract: TruD, a recently discovered novel pseudouridine synthase in Escherichia coli, is responsible for modifying uridine13 in tRNA(Glu) to pseudouridine. It has little sequence homology with the other 10 pseudouridine synthases in E. coli which themselves have been grouped into four related protein families. Crystal structure determination of TruD revealed a two domain structure consisting of a catalytic domain that differs in sequence but is structurally very similar to the catalytic domain of other pseudouridine synthases and a second large domain (149 amino acids, 43% of total) with a novel alpha/beta fold that up to now has not been found in any other protein.
PubMed: 14999002
DOI: 10.1074/jbc.C400072200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 1si7
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2026-02-04に公開中

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