2ggd
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CP4 EPSP synthase Ala100Gly liganded with S3P and Glyphosate
OverviewOverview
The engineering of transgenic crops resistant to the broad-spectrum, herbicide glyphosate has greatly improved agricultural efficiency, worldwide. Glyphosate-based herbicides, such as Roundup, target the, shikimate pathway enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP), synthase, the functionality of which is absolutely required for the, survival of plants. Roundup Ready plants carry the gene coding for a, glyphosate-insensitive form of this enzyme, obtained from Agrobacterium, sp. strain CP4. Once incorporated into the plant genome, the gene product, CP4 EPSP synthase, confers crop resistance to glyphosate. Although widely, used, the molecular basis for this glyphosate-resistance has remained, obscure. We generated a synthetic gene coding for CP4 EPSP synthase and, characterized the enzyme using kinetics and crystallography. The CP4, enzyme has unexpected kinetic and structural properties that render it, unique among the known EPSP synthases. Glyphosate binds to the CP4 EPSP, synthase in a condensed, noninhibitory conformation. Glyphosate, sensitivity can be restored through a single-site mutation in the active, site (Ala-100-Gly), allowing glyphosate to bind in its extended, inhibitory conformation.
About this StructureAbout this Structure
2GGD is a Single protein structure of sequence from Agrobacterium sp. with S3P and GPJ 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 herbicide resistance of Roundup Ready crops., Funke T, Han H, Healy-Fried ML, Fischer M, Schonbrunn E, Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13010-5. Epub 2006 Aug 17. PMID:16916934
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