The structure of chorismate synthase reveals a novel flavin binding to a unique chemical reaction

被引：43

作者：

Maclean, J

Ali, S

机构：

[1] PanTherix Ltd, Dept Biol Struct, Glasgow G20 0XP, Lanark, Scotland

[2] PanTherix Ltd, Dept Biol, Glasgow G20 0XP, Lanark, Scotland

来源：

STRUCTURE | 2003年 / 11卷 / 12期

关键词：

D O I：

10.1016/j.str.2003.11.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of chorismate synthase (CS) from Streptococcus pneumoniae has been solved to 2.0 Angstrom resolution in the presence of flavin mononucleotide (FMN) and the substrate 5-enolpyruvyl-3-shikimate phosphate (EPSP). CS catalyses the final step of the shikimate pathway and is a potential therapeutic target for the rational design of novel antibacterials, antifungals, antiprotozoals, and herbicides. CS is a tetramer with the monomer possessing a novel beta-alpha-beta fold. The interactions between the enzyme, cofactor , and substrate reveal the structural reasons underlying the unique catalytic mechanism and identify the amino acids involved. This structure provides the essential initial information necessary for the generation of novel anti-infective compounds by a structure-guided medicinal chemistry approach.

引用

页码：1499 / 1511

页数：13

共 37 条

[1] The Protein Data Bank [J].