1YY3

Structure of S-Adenosylmethionine:tRNA Ribosyltransferase-Isomerase (QueA)

1YY3 の概要

• エントリーDOI: 10.2210/pdb1yy3/pdb
• 分子名称: S-adenosylmethionine:tRNA ribosyltransferase-isomerase (1 entity in total)
• 機能のキーワード: beta-barrel, quea, bacillus subtilis, quein queuosine, s-adenosylmethionine:trna ribosyltransferase-isomerase, trna-modification, isomerase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm (By similarity): O32054
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77680.08

構造登録者

Grimm, C.,Ficner, R.,Reuter, K. (登録日: 2005-02-23, 公開日: 2006-03-21, 最終更新日: 2024-03-13)

主引用文献

Grimm, C.,Ficner, R.,Sgraja, T.,Haebel, P.,Klebe, G.,Reuter, K.
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase
Biochem.Biophys.Res.Commun., 351:695-701, 2006

PubMed Abstract: The enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) is involved in the biosynthesis of the hypermodified tRNA nucleoside queuosine. It is unprecedented in nature as it uses the cofactor S-adenosylmethionine as the donor of a ribosyl group. We have determined the crystal structure of Bacillus subtilis QueA at a resolution of 2.9A. The structure reveals two domains representing a 6-stranded beta-barrel and an alpha beta alpha-sandwich, respectively. All amino acid residues invariant in the QueA enzymes of known sequence cluster at the interface of the two domains indicating the localization of the substrate binding region and active center. Comparison of the B. subtilis QueA structure with the structure of QueA from Thermotoga maritima suggests a high domain flexibility of this enzyme.

PubMed: 17083917
DOI: 10.1016/j.bbrc.2006.10.096

実験手法

X-RAY DIFFRACTION (2.88 Å)