4AN4

Crystal structure of the glycosyltransferase SnogD from Streptomyces nogalater

4AN4 の概要

• エントリーDOI: 10.2210/pdb4an4/pdb
• 関連するPDBエントリー: 4AMB 4AMG
• 分子名称: GLYCOSYL TRANSFERASE, DEOXYURIDINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase, glycosyltransferase, polyketide biosynthesis, gt1 family, nogalamycin
• 由来する生物種: STREPTOMYCES NOGALATER
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 168670.78

構造登録者

Claesson, M.,Siitonen, V.,Dobritzsch, D.,Metsa-Ketela, M.,Schneider, G. (登録日: 2012-03-15, 公開日: 2012-09-05, 最終更新日: 2023-12-20)

主引用文献

Claesson, M.,Siitonen, V.,Dobritzsch, D.,Metsa-Ketela, M.,Schneider, G.
Crystal Structure of the Glycosyltransferase Snogd from the Biosynthetic Pathway of the Nogalamycin in Streptomyces Nogalater.
FEBS J., 279:3251-, 2012

PubMed Abstract: The glycosyltransferase SnogD from Streptomyces nogalater transfers a nogalamine moiety to the metabolic intermediate 3',4'-demethoxynogalose-1-hydroxynogalamycinone during the final steps of biosynthesis of the aromatic polyketide nogalamycin. The crystal structure of recombinant SnogD, as an apo-enzyme and with a bound nucleotide, 2-deoxyuridine-5'-diphosphate, was determined to 2.6 Å resolution. Reductive methylation of SnogD was crucial for reproducible preparation of diffraction quality crystals due to creation of an additional intermolecular salt bridge between methylated lysine residue Lys384 and Glu374* from an adjacent molecule in the crystal lattice. SnogD is a dimer both in solution and in the crystal, and the enzyme subunit displays a fold characteristic of the GT-B family of glycosyltransferases. Binding of the nucleotide is associated with rearrangement of two active-site loops. Site-directed mutagenesis shows that two active-site histidine residues, His25 and His301, are critical for the glycosyltransferase activities of SnogD both in vivo and in vitro. The crystal structures and the functional data are consistent with a role for His301 in binding of the diphosphate group of the sugar donor substrate, and a function of His25 as a catalytic base in the glycosyl transfer reaction.

PubMed: 22804797
DOI: 10.1111/J.1742-4658.2012.08711.X

実験手法

X-RAY DIFFRACTION (2.7 Å)