1NLM

CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX

1NLM の概要

• エントリーDOI: 10.2210/pdb1nlm/pdb
• 関連するPDBエントリー: 1FOK
• 分子名称: UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: rossmann fold, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein: P17443
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79705.07

構造登録者

Hu, Y.,Chen, L.,Ha, S.,Gross, B.,Falcone, B.,Walker, D.,Mokhtarzadeh, M.,Walker, S. (登録日: 2003-01-07, 公開日: 2003-02-11, 最終更新日: 2023-08-16)

主引用文献

Hu, Y.,Chen, L.,Ha, S.,Gross, B.,Falcone, B.,Walker, D.,Mokhtarzadeh, M.,Walker, S.
Crystal structure of MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
Proc.Natl.Acad.Sci.USA, 100:845-849, 2003

PubMed Abstract: MurG is an essential glycosyltransferase that forms the glycosidic linkage between N-acetyl muramyl pentapeptide and N-acetyl glucosamine in the biosynthesis of the bacterial cell wall. This enzyme is a member of a major superfamily of NDP-glycosyltransferases for which no x-ray structures containing intact substrates have been reported. Here we present the 2.5-A crystal structure of Escherichia coli MurG in complex with its donor substrate, UDP-GlcNAc. Combined with genomic analysis of other superfamily members and site-specific mutagenesis of E. coli MurG, this structure sheds light on the molecular basis for both donor and acceptor selectivity for the superfamily. This structural analysis suggests that it will be possible to evolve new glycosyltransferases from prototypical superfamily members by varying two key loops while maintaining the overall architecture of the family and preserving key residues.

PubMed: 12538870
DOI: 10.1073/pnas.0235749100

実験手法

X-RAY DIFFRACTION (2.5 Å)