3D0Q

Crystal structure of calG3 from Micromonospora echinospora determined in space group I222

3D0Q の概要

• エントリーDOI: 10.2210/pdb3d0q/pdb
• 関連するPDBエントリー: 3D0R
• 分子名称: Protein CalG3, 3[N-MORPHOLINO]PROPANE SULFONIC ACID (3 entities in total)
• 機能のキーワード: calicheamicin synthesis, glycosyltransferase, enediyne antibiotic, transferase
• 由来する生物種: Micromonospora echinospora
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87194.48

構造登録者

Bitto, E.,Singh, S.,Bingman, C.A.,Wesenberg, G.E.,Phillips Jr., G.N. (登録日: 2008-05-02, 公開日: 2008-06-24, 最終更新日: 2024-11-06)

主引用文献

Zhang, C.,Bitto, E.,Goff, R.D.,Singh, S.,Bingman, C.A.,Griffith, B.R.,Albermann, C.,Phillips, G.N.,Thorson, J.S.
Biochemical and structural insights of the early glycosylation steps in calicheamicin biosynthesis.
Chem.Biol., 15:842-853, 2008

PubMed Abstract: The enediyne antibiotic calicheamicin (CLM) gamma(1)(I) is a prominent antitumor agent that is targeted to DNA by a novel aryltetrasaccharide comprised of an aromatic unit and four unusual carbohydrates. Herein we report the heterologous expression and the biochemical characterization of the two "internal" glycosyltransferases CalG3 and CalG2 and the structural elucidation of an enediyne glycosyltransferase (CalG3). In conjunction with the previous characterization of the "external" CLM GTs CalG1 and CalG4, this study completes the functional assignment of all four CLM GTs, extends the utility of enediyne GT-catalyzed reaction reversibility, and presents conclusive evidence of a sequential glycosylation pathway in CLM biosynthesis. This work also reveals the common GT-B structural fold can now be extended to include enediyne GTs.

PubMed: 18721755
DOI: 10.1016/j.chembiol.2008.06.011

実験手法

X-RAY DIFFRACTION (2.79 Å)