2aa9
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EPSP synthase liganded with shikimate
OverviewOverview
The shikimate pathway enzyme 5-enolpyruvyl shikimate-3-phosphate synthase (EPSP synthase) has received attention in the past because it is the target of the broad-spectrum herbicide glyphosate. The natural substrate of EPSP synthase is shikimate-3-phosphate. However, this enzyme can also utilize shikimate as substrate. Remarkably, this reaction is insensitive to inhibition by glyphosate. Crystallographic analysis of EPSP synthase from Escherichia coli, in complex with shikimate/glyphosate at 1.5 Angstroms resolution, revealed that binding of shikimate induces changes around the backbone of the active site, which in turn impact the efficient binding of glyphosate. The implications from these findings with respect to the design of novel glyphosate-insensitive EPSP synthase enzymes are discussed.
About this StructureAbout this Structure
2AA9 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as 3-phosphoshikimate 1-carboxyvinyltransferase, with EC number 2.5.1.19 Full crystallographic information is available from OCA.
ReferenceReference
Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate., Priestman MA, Healy ML, Funke T, Becker A, Schonbrunn E, FEBS Lett. 2005 Oct 24;579(25):5773-80. PMID:16225867
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