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5UCM

Crystal Structure of Prolyl-tRNA Synthetase from Pseudomonas aeruginosa

5UCM の概要
エントリーDOI10.2210/pdb5ucm/pdb
分子名称Proline--tRNA ligase, MAGNESIUM ION (3 entities in total)
機能のキーワードssgcid, prors, proline-trna ligase, structural genomics, seattle structural genomics center for infectious disease, ligase
由来する生物種Pseudomonas aeruginosa
タンパク質・核酸の鎖数2
化学式量合計128466.48
構造登録者
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2016-12-22, 公開日: 2017-02-22, 最終更新日: 2025-10-22)
主引用文献Pena, N.,Dranow, D.M.,Hu, Y.,Escamilla, Y.,Bullard, J.M.
Characterization and structure determination of prolyl-tRNA synthetase from Pseudomonas aeruginosa and development as a screening platform.
Protein Sci., 2019
Cited by
PubMed Abstract: Pseudomonas aeruginosa is an opportunistic multi-drug resistant pathogen implicated as a causative agent in nosocomial and community acquired bacterial infections. The gene encoding prolyl-tRNA synthetase (ProRS) from P. aeruginosa was overexpressed in Escherichia coli and the resulting protein was characterized. ProRS was kinetically evaluated and the K values for interactions with ATP, proline, and tRNA were 154, 122, and 5.5 μM, respectively. The turn-over numbers, k , for interactions with these substrates were calculated to be 5.5, 6.3, and 0.2 s , respectively. The crystal structure of the α form of P. aeruginosa ProRS was solved to 2.60 Å resolution. The amino acid sequence and X-ray crystal structure of P. aeruginosa ProRS was analyzed and compared with homologs in which the crystal structures have been solved. The amino acids that interact with ATP and proline are well conserved in the active site region and overlay of the crystal structure with ProRS homologs conforms to a similar overall three-dimensional structure. ProRS was developed into a screening platform using scintillation proximity assay (SPA) technology and used to screen 890 chemical compounds, resulting in the identification of two inhibitory compounds, BT06A02 and BT07H05. This work confirms the utility of a screening system based on the functionality of ProRS from P. aeruginosa.
PubMed: 30666738
DOI: 10.1002/pro.3579
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 5ucm
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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