6EI9

Crystal structure of E. coli tRNA-dihydrouridine synthase B (DusB)

6EI9 の概要

• エントリーDOI: 10.2210/pdb6ei9/pdb
• 分子名称: tRNA-dihydrouridine synthase B, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, trna modification, rna binding protein, flavoprotein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77994.29

構造登録者

Bou-Nader, C.,Hamdane, D. (登録日: 2017-09-18, 公開日: 2018-01-17, 最終更新日: 2024-01-17)

主引用文献

Bou-Nader, C.,Montemont, H.,Guerineau, V.,Jean-Jean, O.,Bregeon, D.,Hamdane, D.
Unveiling structural and functional divergences of bacterial tRNA dihydrouridine synthases: perspectives on the evolution scenario.
Nucleic Acids Res., 46:1386-1394, 2018

PubMed Abstract: Post-transcriptional base modifications are important to the maturation process of transfer RNAs (tRNAs). Certain modifications are abundant and present at several positions in tRNA as for example the dihydrouridine, a modified base found in the three domains of life. Even though the function of dihydrourine is not well understood, its high content in tRNAs from psychrophilic bacteria or cancer cells obviously emphasizes a central role in cell adaptation. The reduction of uridine to dihydrouridine is catalyzed by a large family of flavoenzymes named dihydrouridine synthases (Dus). Prokaryotes have three Dus (A, B and C) wherein DusB is considered as an ancestral protein from which the two others derived via gene duplications. Here, we unequivocally established the complete substrate specificities of the three Escherichia coli Dus and solved the crystal structure of DusB, enabling for the first time an exhaustive structural comparison between these bacterial flavoenzymes. Based on our results, we propose an evolutionary scenario explaining how substrate specificities has been diversified from a single structural fold.

PubMed: 29294097
DOI: 10.1093/nar/gkx1294

実験手法

X-RAY DIFFRACTION (2.55 Å)