2OHC

structural and mutational analysis of tRNA-intron splicing endonuclease from Thermoplasma acidophilum DSM1728

2OHC の概要

• エントリーDOI: 10.2210/pdb2ohc/pdb
• 関連するPDBエントリー: 2ohe
• 分子名称: tRNA-splicing endonuclease (2 entities in total)
• 機能のキーワード: trna, intron, splicing, endonuclease, hydrolase
• 由来する生物種: Thermoplasma acidophilum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66513.27

構造登録者

Kim, Y.K.,Mizutani, K.,Rhee, K.H.,Lee, W.H.,Park, S.Y.,Hwang, K.Y. (登録日: 2007-01-10, 公開日: 2007-11-27, 最終更新日: 2024-10-30)

主引用文献

Kim, Y.K.,Mizutani, K.,Rhee, K.H.,Nam, K.H.,Lee, W.H.,Lee, E.H.,Kim, E.E.,Park, S.Y.,Hwang, K.Y.
Structural and Mutational Analysis of tRNA Intron-Splicing Endonuclease from Thermoplasma acidophilum DSM 1728: Catalytic Mechanism of tRNA Intron-Splicing Endonucleases
J.Bacteriol., 189:8339-8346, 2007

PubMed Abstract: In archaea, RNA endonucleases that act specifically on RNA with bulge-helix-bulge motifs play the main role in the recognition and excision of introns, while the eukaryal enzymes use a measuring mechanism to determine the positions of the universally positioned splice sites relative to the conserved domain of pre-tRNA. Two crystallographic structures of tRNA intron-splicing endonuclease from Thermoplasma acidophilum DSM 1728 (EndA(Ta)) have been solved to 2.5-A and 2.7-A resolution by molecular replacement, using the 2.7-A resolution data as the initial model and the single-wavelength anomalous-dispersion phasing method using selenomethionine as anomalous signals, respectively. The models show that EndA(Ta) is a homodimer and that it has overall folding similar to that of other archaeal tRNA endonucleases. From structural and mutational analyses of H236A, Y229F, and K265I in vitro, we have demonstrated that they play critical roles in recognizing the splice site and in cleaving the pre-tRNA substrate.

PubMed: 17827289
DOI: 10.1128/JB.00713-07

実験手法

X-RAY DIFFRACTION (2.5 Å)