5ZTB
Structure of Sulfurtransferase
5ZTB の概要
エントリーDOI | 10.2210/pdb5ztb/pdb |
分子名称 | Sulfur carrier protein TtuB, tRNA-5-methyluridine(54) 2-sulfurtransferase, GLYCEROL, ... (8 entities in total) |
機能のキーワード | sulfur transfer, iron-sulfur cluster, trna binding protein, complex, rna binding protein, rna binding protein-transferase complex, rna binding protein/transferase |
由来する生物種 | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 137628.44 |
構造登録者 | |
主引用文献 | Chen, M.,Ishizaka, M.,Narai, S.,Horitani, M.,Shigi, N.,Yao, M.,Tanaka, Y. The [4Fe-4S] cluster of sulfurtransferase TtuA desulfurizes TtuB during tRNA modification in Thermus thermophilus. Commun Biol, 3:168-168, 2020 Cited by PubMed Abstract: TtuA and TtuB are the sulfurtransferase and sulfur donor proteins, respectively, for biosynthesis of 2-thioribothymidine (sT) at position 54 of transfer RNA (tRNA), which is responsible for adaptation to high temperature environments in Thermus thermophilus. The enzymatic activity of TtuA requires an iron-sulfur (Fe-S) cluster, by which a sulfur atom supplied by TtuB is transferred to the tRNA substrate. Here, we demonstrate that the Fe-S cluster directly receives sulfur from TtuB through its inherent coordination ability. TtuB forms a [4Fe-4S]-TtuB intermediate, but that sulfur is not immediately released from TtuB. Further desulfurization assays and mutation studies demonstrated that the release of sulfur from the thiocarboxylated C-terminus of TtuB is dependent on adenylation of the substrate tRNA, and the essential residue for TtuB desulfurization was identified. Based on these findings, the molecular mechanism of sulfur transfer from TtuB to Fe-S cluster is proposed. PubMed: 32265486DOI: 10.1038/s42003-020-0895-3 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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