2IV3

Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis

2IV3 の概要

• エントリーDOI: 10.2210/pdb2iv3/pdb
• 関連するPDBエントリー: 2IUY
• 分子名称: GLYCOSYLTRANSFERASE, URIDINE-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, transferase, antibiotics, family gt-4, avilamycin a
• 由来する生物種: STREPTOMYCES VIRIDOCHROMOGENES
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 146548.74

構造登録者

Martinez-Fleites, C.,Proctor, M.,Roberts, S.,Bolam, D.N.,Gilbert, H.J.,Davies, G.J. (登録日: 2006-06-08, 公開日: 2006-10-11, 最終更新日: 2023-12-13)

主引用文献

Martinez-Fleites, C.,Proctor, M.,Roberts, S.,Bolam, D.N.,Gilbert, H.J.,Davies, G.J.
Insights Into the Synthesis of Lipopolysaccharide and Antibiotics Through the Structures of Two Retaining Glycosyltransferases from Family Gt4
Chem.Biol., 13:1143-, 2006

PubMed Abstract: Glycosyltransferases (GTs) catalyze the synthesis of the myriad glycoconjugates that are central to life. One of the largest families is GT4, which contains several enzymes of therapeutic significance, exemplified by WaaG and AviGT4. WaaG catalyses a key step in lipopolysaccharide synthesis, while AviGT4, produced by Streptomyces viridochromogenes, contributes to the synthesis of the antibiotic avilamycin A. Here we present the crystal structure of both WaaG and AviGT4. The two enzymes contain two "Rossmann-like" (beta/alpha/beta) domains characteristic of the GT-B fold. Both recognition of the donor substrate and the catalytic machinery is similar to other retaining GTs that display the GT-B fold. Structural information is discussed with respect to the evolution of GTs and the therapeutic significance of the two enzymes.

PubMed: 17113996
DOI: 10.1016/J.CHEMBIOL.2006.09.005

実験手法

X-RAY DIFFRACTION (2.3 Å)