2GGD

CP4 EPSP synthase Ala100Gly liganded with S3P and Glyphosate

Summary for 2GGD

• Entry DOI: 10.2210/pdb2ggd/pdb
• Related: 1G6S 1G6T 1MI4 1Q36 1RF5 1RF6 2GG4 2GG6 2GGA
• Descriptor: 3-phosphoshikimate 1-carboxyvinyltransferase, SHIKIMATE-3-PHOSPHATE, GLYPHOSATE, ... (4 entities in total)
• Functional Keywords: inside-out alpha/beta barrel; two domain structure, transferase
• Biological source: Agrobacterium sp.
• Cellular location: Cytoplasm (Probable): Q9R4E4
• Total number of polymer chains: 1
• Total formula weight: 48047.52

Authors

Schonbrunn, E.,Funke, T. (deposition date: 2006-03-23, release date: 2006-08-22, Last modification date: 2023-08-30)

Primary citation

Funke, T.,Han, H.,Healy-Fried, M.L.,Fischer, M.,Schonbrunn, E.
Molecular basis for the herbicide resistance of Roundup Ready crops.
Proc.Natl.Acad.Sci.Usa, 103:13010-13015, 2006

PubMed Abstract: 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.

PubMed: 16916934
DOI: 10.1073/pnas.0603638103

Experimental method

X-RAY DIFFRACTION (1.7 Å)