5MKO
[2Fe-2S] cluster containing TtuA in complex with AMP.
5MKO の概要
| エントリーDOI | 10.2210/pdb5mko/pdb |
| 関連するPDBエントリー | 3VRH |
| 分子名称 | TtuA PH0300, ADENOSINE MONOPHOSPHATE, ZINC ION, ... (5 entities in total) |
| 機能のキーワード | ttua, ph0300, amp, 2fe-2s, thiolation, trna modification enzyme, [fe-s] cluster, iron-sulfur cluster, rna |
| 由来する生物種 | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 73153.47 |
| 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 Cited by 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: 28655838DOI: 10.1073/pnas.1700902114 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.65 Å) |
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