Interaction of the herbicide glyphosate with its target enzyme 
5-enolpyruvylshikimate 3-phosphate synthase in atomic detail

Schönbrunn, Ernst; Eschenburg, Susanne; Shuttleworth, Wendy A.; Schloss, John V.; Amrhein, Nikolaus; Evans, Jeremy N. S.; Kabsch, Wolfgang

doi:10.1073/pnas.98.4.1376

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail

MPS-Authors

/persons/resource/persons92829

Eschenburg, Susanne
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93650

Kabsch, Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://dx.doi.org/10.1073/pnas.98.4.1376
(全文テキスト（全般）)

http://www.pnas.org/content/98/4/1376.full.pdf
(全文テキスト（全般）)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Schönbrunn, E., Eschenburg, S., Shuttleworth, W. A., Schloss, J. V., Amrhein, N., Evans, J. N. S., & Kabsch, W. (2001). Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proceedings of the National Academy of Sciences of the United States of America, 98(4), 1376-1380. doi:10.1073/pnas.98.4.1376.

引用: https://hdl.handle.net/11858/00-001M-0000-0029-1F62-8

要旨

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.