1G6T

STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE

Summary for 1G6T

• Entry DOI: 10.2210/pdb1g6t/pdb
• Related: 1G6S
• Descriptor: EPSP SYNTHASE, PHOSPHATE ION, SHIKIMATE-3-PHOSPHATE, ... (5 entities in total)
• Functional Keywords: two-domain structure; inside-out alpha-beta barrel, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A6D3
• Total number of polymer chains: 1
• Total formula weight: 47089.04

Authors

Schonbrunn, E.,Eschenburg, S.,Shuttleworth, W.,Schloss, J.V.,Amrhein, N.,Evans, J.N.S.,Kabsch, W. (deposition date: 2000-11-07, release date: 2001-02-07, Last modification date: 2024-02-07)

Primary citation

Schonbrunn, E.,Eschenburg, S.,Shuttleworth, W.A.,Schloss, J.V.,Amrhein, N.,Evans, J.N.,Kabsch, W.
Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail.
Proc.Natl.Acad.Sci.USA, 98:1376-1380, 2001

PubMed Abstract: Biosynthesis of aromatic amino acids in plants, many bacteria, and microbes relies on the enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase, a prime target for drugs and herbicides. We have identified the interaction of EPSP synthase with one of its two substrates (shikimate 3-phosphate) and with the widely used herbicide glyphosate by x-ray crystallography. The two-domain enzyme closes on ligand binding, thereby forming the active site in the interdomain cleft. Glyphosate appears to occupy the binding site of the second substrate of EPSP synthase (phosphoenol pyruvate), mimicking an intermediate state of the ternary enzyme.substrates complex. The elucidation of the active site of EPSP synthase and especially of the binding pattern of glyphosate provides a valuable roadmap for engineering new herbicides and herbicide-resistant crops, as well as new antibiotic and antiparasitic drugs.

PubMed: 11171958
DOI: 10.1073/pnas.98.4.1376

Experimental method

X-RAY DIFFRACTION (1.6 Å)