2I4M

Rhodopseudomonas palustris prolyl-tRNA synthetase in complex with ProAMS

2I4M の概要

• エントリーDOI: 10.2210/pdb2i4m/pdb
• 分子名称: Proline-tRNA ligase, '5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE (3 entities in total)
• 機能のキーワード: alpha beta, ligase
• 由来する生物種: Rhodopseudomonas palustris
• 細胞内の位置: Cytoplasm: Q6N5P6
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 155523.26

構造登録者

Crepin, T.,Yaremchuk, A.,Tukalo, M.,Cusack, S. (登録日: 2006-08-22, 公開日: 2006-10-24, 最終更新日: 2023-08-16)

主引用文献

Crepin, T.,Yaremchuk, A.,Tukalo, M.,Cusack, S.
Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain.
Structure, 14:1511-1525, 2006

PubMed Abstract: Prolyl-tRNA synthetases (ProRSs) are unique among synthetases in that they have diverse architectures, notably the variable presence of a cis-editing domain homologous to the freestanding deacylase proteins YbaK and ProX. Here, we describe crystal structures of two bacterial ProRSs from the pathogen Enterococcus faecalis, which possesses an editing domain, and from Rhodopseudomonas palustris, which does not. We compare the overall structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus. Although structurally more homologous to YbaK, which preferentially hydrolyzes Cys-tRNA(Pro), the editing domain of E. faecalis ProRS possesses key elements similar to ProX, with which it shares the activity of hydrolyzing Ala-tRNA(Pro). The structures give insight into the complex evolution of ProRSs, the mechanism of editing, and structural differences between prokaryotic- and eukaryotic-type ProRSs that can be exploited for antibiotic design.

PubMed: 17027500
DOI: 10.1016/j.str.2006.08.007

実験手法

X-RAY DIFFRACTION (2.8 Å)