3RSC

Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP and calicheamicin T0 bound form

3RSC の概要

• エントリーDOI: 10.2210/pdb3rsc/pdb
• 関連するPDBエントリー: 3IAA
• 分子名称: CalG2, THYMIDINE-5'-DIPHOSPHATE, Calicheamicin T0, ... (5 entities in total)
• 機能のキーワード: tdp, enediyne, structural genomics, psi-2, protein structure initiative, center for eukaryotic structural genomics, cesg, glycosyltransferase, transferase-antibiotic complex, enzyme discovery for natural product biosynthesis, natpro, transferase/antibiotic
• 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: 94010.23

構造登録者

Chang, A.,Helmich, K.E.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG),Enzyme Discovery for Natural Product Biosynthesis (NatPro) (登録日: 2011-05-02, 公開日: 2011-08-10, 最終更新日: 2024-10-30)

主引用文献

Chang, A.,Singh, S.,Helmich, K.E.,Goff, R.D.,Bingman, C.A.,Thorson, J.S.,Phillips, G.N.
Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity.
Proc.Natl.Acad.Sci.USA, 108:17649-17654, 2011

PubMed Abstract: Glycosyltransferases are useful synthetic catalysts for generating natural products with sugar moieties. Although several natural product glycosyltransferase structures have been reported, design principles of glycosyltransferase engineering for the generation of glycodiversified natural products has fallen short of its promise, partly due to a lack of understanding of the relationship between structure and function. Here, we report structures of all four calicheamicin glycosyltransferases (CalG1, CalG2, CalG3, and CalG4), whose catalytic functions are clearly regiospecific. Comparison of these four structures reveals a conserved sugar donor binding motif and the principles of acceptor binding region reshaping. Among them, CalG2 possesses a unique catalytic motif for glycosylation of hydroxylamine. Multiple glycosyltransferase structures in a single natural product biosynthetic pathway are a valuable resource for understanding regiospecific reactions and substrate selectivities and will help future glycosyltransferase engineering.

PubMed: 21987796
DOI: 10.1073/pnas.1108484108

実験手法

X-RAY DIFFRACTION (2.19 Å)