2Z2U

Crystal structure of archaeal TYW1

2Z2U の概要

• エントリーDOI: 10.2210/pdb2z2u/pdb
• 分子名称: UPF0026 protein MJ0257 (2 entities in total)
• 機能のキーワード: metal binding protein
• 由来する生物種: Methanocaldococcus jannaschii
• 細胞内の位置: Cytoplasm (Potential): Q57705
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36770.83

構造登録者

Suzuki, Y.,Ishitani, R.,Nureki, O. (登録日: 2007-05-28, 公開日: 2007-10-23, 最終更新日: 2024-03-13)

主引用文献

Suzuki, Y.,Noma, A.,Suzuki, T.,Senda, M.,Senda, T.,Ishitani, R.,Nureki, O.
Crystal Structure of the Radical SAM Enzyme Catalyzing Tricyclic Modified Base Formation in tRNA
J.Mol.Biol., 372:1204-1214, 2007

PubMed Abstract: Wyosine and its derivatives, such as wybutosine, found in eukaryotic and archaeal tRNAs, are tricyclic hypermodified nucleosides. In eukaryotes, wybutosine exists exclusively in position 37, 3'-adjacent to the anticodon, of tRNA(Phe), where it ensures correct translation by stabilizing the codon-anticodon base-pairing during the ribosomal decoding process. Recent studies revealed that the wyosine biosynthetic pathway consists of multistep enzymatic reactions starting from a guanosine residue. Among these steps, TYW1 catalyzes the second step to form the tricyclic ring structure, by cyclizing N(1)-methylguanosine. In this study, we solved the crystal structure of TYW1 from Methanocaldococcus jannaschii at 2.4 A resolution. TYW1 assumes an incomplete TIM barrel with (alpha/beta)(6) topology, which closely resembles the reported structures of radical SAM enzymes. Hence, TYW1 was considered to catalyze the cyclization reaction by utilizing the radical intermediate. Comparison with other radical SAM enzymes allowed us to build a model structure complexed with S-adenosylmethionine and two [4Fe-4S] clusters. Mutational analyses in yeast supported the validity of this complex model structure, which provides a structural insight into the radical reaction involving two [4Fe-4S] clusters to create a complex tricyclic base.

PubMed: 17727881
DOI: 10.1016/j.jmb.2007.07.024

実験手法

X-RAY DIFFRACTION (2.4 Å)