1qxo
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(New page: 200px<br /><applet load="1qxo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qxo, resolution 2.0Å" /> '''Crystal structure of ...)
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Revision as of 22:58, 20 November 2007
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Crystal structure of Chorismate synthase complexed with oxidized FMN and EPSP
Overview
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 Structure
1QXO is a Single protein structure of sequence from Streptococcus pneumoniae with NCO, EDO, FMN and EPS as ligands. Active as Chorismate synthase, with EC number 4.2.3.5 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 01:05:53 2007
Categories: Chorismate synthase | Single protein | Streptococcus pneumoniae | Ali, S. | Maclean, J. | EDO | EPS | FMN | NCO | Anti-infective | Beta-alpha-beta | Flavoprotein | Shikimate
