4YDU

Crystal structure of E. coli YgjD-YeaZ heterodimer in complex with ADP

「4WOS」から置き換えられました

4YDU の概要

• エントリーDOI: 10.2210/pdb4ydu/pdb
• 分子名称: tRNA N6-adenosine threonylcarbamoyltransferase, tRNA threonylcarbamoyladenosine biosynthesis protein TsaB, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: ygjd-yeaz complex, t6a transferase, transferase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm : P05852 P76256
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 128462.42

構造登録者

Zhang, W.,Collinet, B.,Perrochia, L.,Durand, D.,Van Tilbeurgh, H. (登録日: 2015-02-23, 公開日: 2015-03-04, 最終更新日: 2024-01-10)

主引用文献

Zhang, W.,Collinet, B.,Perrochia, L.,Durand, D.,Van Tilbeurgh, H.
The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli.
Nucleic Acids Res., 43:1804-1817, 2015

PubMed Abstract: The essential and universal N(6)-threonylcarbamoyladenosine (t(6)A) modification at position 37 of ANN-decoding tRNAs plays a pivotal role in translational fidelity through enhancement of the cognate codon recognition and stabilization of the codon-anticodon interaction. In Escherichia coli, the YgjD (TsaD), YeaZ (TsaB), YjeE (TsaE) and YrdC (TsaC) proteins are necessary and sufficient for the in vitro biosynthesis of t(6)A, using tRNA, ATP, L-threonine and bicarbonate as substrates. YrdC synthesizes the short-lived L-threonylcarbamoyladenylate (TCA), and YgjD, YeaZ and YjeE cooperate to transfer the L-threonylcarbamoyl-moiety from TCA onto adenosine at position 37 of substrate tRNA. We determined the crystal structure of the heterodimer YgjD-YeaZ at 2.3 Å, revealing the presence of an unexpected molecule of ADP bound at an atypical site situated at the YgjD-YeaZ interface. We further showed that the ATPase activity of YjeE is strongly activated by the YgjD-YeaZ heterodimer. We established by binding experiments and SAXS data analysis that YgjD-YeaZ and YjeE form a compact ternary complex only in presence of ATP. The formation of the ternary YgjD-YeaZ-YjeE complex is required for the in vitro biosynthesis of t(6)A but not its ATPase activity.

PubMed: 25578970
DOI: 10.1093/nar/gku1397

実験手法

X-RAY DIFFRACTION (2.33 Å)