1UDQ

Crystal structure of the tRNA processing enzyme RNase PH T125A mutant from Aquifex aeolicus

1UDQ の概要

• エントリーDOI: 10.2210/pdb1udq/pdb
• 関連するPDBエントリー: 1UDN 1UDO 1UDS
• 分子名称: Ribonuclease PH, PHOSPHATE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transferase, riken structural genomics/proteomics initiative, rsgi, structural genomics
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28665.53

構造登録者

Ishii, R.,Nureki, O.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-05-02, 公開日: 2003-09-23, 最終更新日: 2023-12-27)

主引用文献

Ishii, R.,Nureki, O.,Yokoyama, S.
Crystal Structure of the tRNA Processing Enzyme RNase PH from Aquifex aeolicus
J.Biol.Chem., 278:32397-32404, 2003

PubMed Abstract: RNase PH is one of the exoribonucleases that catalyze the 3' end processing of tRNA in bacteria. RNase PH removes nucleotides following the CCA sequence of tRNA precursors by phosphorolysis and generates mature tRNAs with amino acid acceptor activity. In this study, we determined the crystal structure of Aquifex aeolicus RNase PH bound with a phosphate, a co-substrate, in the active site at 2.3-A resolution. RNase PH has the typical alpha/beta fold, which forms a hexameric ring structure as a trimer of dimers. This ring structure resembles that of the polynucleotide phosphorylase core domain homotrimer, another phosphorolytic exoribonuclease. Four amino acid residues, Arg-86, Gly-124, Thr-125, and Arg-126, of RNase PH are involved in the phosphate-binding site. Mutational analyses of these residues showed their importance in the phosphorolysis reaction. A docking model with the tRNA acceptor stem suggests how RNase PH accommodates substrate RNAs.

PubMed: 12746447
DOI: 10.1074/jbc.M300639200

実験手法

X-RAY DIFFRACTION (2.3 Å)