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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biophysik     Display Documents

ID: 22943.0, MPI für medizinische Forschung / Abteilung Biophysik
Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail
Translation of Title:Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail
Authors:Schönbrunn, Ernst; Eschenburg, Susanne; Shuttleworth, Wendy A.; Schloss, John V.; Amrhein, Nikolaus; Evans, Jeremy N. S.; Kabsch, Wolfgang
Date of Publication (YYYY-MM-DD):2001-02-13
Title of Journal:PNAS Online 1990 - Present
Journal Abbrev.:Proc. Natl. Acad. Sci. U. S. A.
Issue / Number:4
Start Page:1376
End Page:1380
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik/
Identifiers:URI: [Full text]
URI: [Abstract]
URI: [Fulltext PDF]
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