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  How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli

Eschenburg, S., Healy, M. L., Priestman, M. A., Lushington, G. H., & Schönbrunn, E. (2002). How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli. Planta, 216(1), 129-135. doi:10.1007/s00425-002-0908-0.

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Genre: Journal Article
Alternative Title : How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli

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Eschenburg, Susanne1, Author              
Healy, Martha L., Author
Priestman, Melanie A., Author
Lushington, Gerald H., Author
Schönbrunn, Ernst, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: 5-Enoylpyruvyl shikimate-3-phosphate synthase; Glyphosate; Herbicide resistance; Molecular modeling; X-ray crystallography
 Abstract: The enzyme 5-enolpyruvyl shikimate-3-phosphate (EPSP) synthase (EC 2.5.1.19) is essential for the biosynthesis of aromatic compounds in plants and microbes and is the unique target of the herbicide glyphosate. One of the first glyphosate-insensitive enzymes reported was a Gly96Ala mutant of EPSP synthase from Klebsiella pneumoniae. We have introduced this single-site mutation into the highly homologous EPSP synthase from Escherichia coli. The mutant enzyme is insensitive to glyphosate with unaltered affinity for its first substrate, shikimate-3-phosphate (S3P), but displays a 30-fold lower affinity for its second substrate, phosphoenolpyruvate (PEP). Using X-ray crystallography, we solved the structure of Gly96Ala-EPSP synthase liganded with S3P to 0.17 nm resolution. The crystal structure shows that the additional methyl group from Ala96 protrudes into the active site of the enzyme. While the interactions between enzyme and S3P remain unaffected, the accessible volume for glyphosate binding is substantially reduced. Exploiting the crystallographic results for molecular modeling, we demonstrate that PEP but not glyphosate can be docked in the Gly96Ala-modified binding site. The predicted PEP binding site satisfies the earlier proposed interaction pattern for PEP with EPSP synthase and corroborates the assumption that glyphosate and PEP target the same binding site.

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Language(s): eng - English
 Dates: 2002-07-102002-08-262002-11-122002-11-12
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665828
DOI: 10.1007/s00425-002-0908-0
URI: http://www.ncbi.nlm.nih.gov/pubmed/12430021
Other: 6072
 Degree: -

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Title: Planta
Source Genre: Journal
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Publ. Info: Berlin : Springer-Verlag
Pages: - Volume / Issue: 216 (1) Sequence Number: - Start / End Page: 129 - 135 Identifier: ISSN: 0032-0935
CoNE: https://pure.mpg.de/cone/journals/resource/954925434427