Crystal structure of Chorismate synthase complexed with oxidized FMN and EPSP

File:1qxo.jpg


1qxo, resolution 2.0Å

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OverviewOverview

The crystal structure of chorismate synthase (CS) from Streptococcus pneumoniae has been solved to 2.0 A 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.

About this StructureAbout this Structure

1QXO is a Single protein structure of sequence from Streptococcus pneumoniae with , , and as ligands. Active as Chorismate synthase, with EC number 4.2.3.5 Full crystallographic information is available from OCA.

ReferenceReference

The structure of chorismate synthase reveals a novel flavin binding site fundamental to a unique chemical reaction., Maclean J, Ali S, Structure. 2003 Dec;11(12):1499-511. PMID:14656434

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