5MKP

Non redox thiolation in transfer RNAs occuring via sulfur activation by a [4Fe-4S] cluster

5MKP の概要

• エントリーDOI: 10.2210/pdb5mkp/pdb
• 関連するPDBエントリー: 3VRH
• 分子名称: PH0300, ZINC ION, Fe4 H S5, ... (4 entities in total)
• 機能のキーワード: ttua, [4fe-5s], sulfur insertion, trna modification, thiolation reaction, iron-sulfur cluster, rna
• 由来する生物種: Pyrococcus horikoshii OT3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36438.41

構造登録者

Arragain, S.,Bimai, O.,Legrand, P.,Golinelli-Pimpaneau, B. (登録日: 2016-12-05, 公開日: 2017-06-14, 最終更新日: 2024-01-17)

主引用文献

Arragain, S.,Bimai, O.,Legrand, P.,Caillat, S.,Ravanat, J.L.,Touati, N.,Binet, L.,Atta, M.,Fontecave, M.,Golinelli-Pimpaneau, B.
Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster.
Proc. Natl. Acad. Sci. U.S.A., 114:7355-7360, 2017

PubMed Abstract: Sulfur is present in several nucleosides within tRNAs. In particular, thiolation of the universally conserved methyl-uridine at position 54 stabilizes tRNAs from thermophilic bacteria and hyperthermophilic archaea and is required for growth at high temperature. The simple nonredox substitution of the C2-uridine carbonyl oxygen by sulfur is catalyzed by tRNA thiouridine synthetases called TtuA. Spectroscopic, enzymatic, and structural studies indicate that TtuA carries a catalytically essential [4Fe-4S] cluster and requires ATP for activity. A series of crystal structures shows that () the cluster is ligated by only three cysteines that are fully conserved, allowing the fourth unique iron to bind a small ligand, such as exogenous sulfide, and () the ATP binding site, localized thanks to a protein-bound AMP molecule, a reaction product, is adjacent to the cluster. A mechanism for tRNA sulfuration is suggested, in which the unique iron of the catalytic cluster serves to bind exogenous sulfide, thus acting as a sulfur carrier.

PubMed: 28655838
DOI: 10.1073/pnas.1700902114

実験手法

X-RAY DIFFRACTION (2.5 Å)