1EFZ

MUTAGENESIS AND CRYSTALLOGRAPHIC STUDIES OF ZYMOMONAS MOBILIS TRNA-GUANINE TRANSGLYCOSYLASE TO ELUCIDATE THE ROLE OF SERINE 103 FOR ENZYMATIC ACTIVITY

1EFZ の概要

• エントリーDOI: 10.2210/pdb1efz/pdb
• 関連するPDBエントリー: 1pud
• 分子名称: TRNA-GUANINE TRANSGLYCOSYLASE, ZINC ION, 7-DEAZA-7-AMINOMETHYL-GUANINE, ... (4 entities in total)
• 機能のキーワード: trna-modifying enzyme, transferase, glycosyltransferase
• 由来する生物種: Zymomonas mobilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43154.29

構造登録者

Gradler, U.,Ficner, R.,Garcia, G.A.,Stubbs, M.T.,Klebe, G.,Reuter, K. (登録日: 2000-02-11, 公開日: 2000-03-01, 最終更新日: 2024-02-07)

主引用文献

Gradler, U.,Ficner, R.,Garcia, G.A.,Stubbs, M.T.,Klebe, G.,Reuter, K.
Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity.
FEBS Lett., 454:142-146, 1999

PubMed Abstract: The tRNA modifying enzyme tRNA-guanine transglycosylase (TGT) is involved in the exchange of guanine in the first position of the anticodon with preQ1 as part of the biosynthesis of the hypermodified base queuine (Q). Mutation of Ser90 to an alanine in Escherichia coli TGT leads to a dramatic reduction of enzymatic activity (Reuter, K. et al. (1994) Biochemistry 33, 7041-7046). To further clarify the role of this residue in the catalytic center, we have mutated the corresponding Ser103 of the crystallizable Zymomonas mobilis TGT into alanine. The crystal structure of a TGT(S103A)/preQ1 complex combined with biochemical data presented in this paper suggest that Ser103 is essential for substrate orientation in the TGT reaction.

PubMed: 10413112
DOI: 10.1016/S0014-5793(99)00793-0

実験手法

X-RAY DIFFRACTION (2 Å)