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2qfq

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{{STRUCTURE_2qfq| PDB=2qfq | SCENE= }}
{{STRUCTURE_2qfq| PDB=2qfq | SCENE= }}
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'''E. coli EPSP synthase Pro101Leu liganded with S3P'''
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===E. coli EPSP synthase Pro101Leu liganded with S3P===
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==Overview==
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Glyphosate, the world's most used herbicide, is a massive success because it enables efficient weed control with minimal animal and environmental toxicity. The molecular target of glyphosate is 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), which catalyzes the sixth step of the shikimate pathway in plants and microorganisms. Glyphosate-tolerant variants of EPSPS constitute the basis of genetically engineered herbicide-tolerant crops. A single-site mutation of Pro(101) in EPSPS (numbering according to the enzyme from Escherichia coli) has been implicated in glyphosate-resistant weeds, but this residue is not directly involved in glyphosate binding, and the basis for this phenomenon has remained unclear in the absence of further kinetic and structural characterization. To probe the effects of mutations at this site, E. coli EPSPS enzymes were produced with glycine, alanine, serine, or leucine substituted for Pro(101). These mutant enzymes were analyzed by steady-state kinetics, and the crystal structures of the substrate binary and substrate.glyphosate ternary complexes of P101S and P101L EPSPS were determined to between 1.5- and 1.6-A resolution. It appears that residues smaller than leucine may be substituted for Pro(101) without decreasing catalytic efficiency. Any mutation at this site results in a structural change in the glyphosate-binding site, shifting Thr(97) and Gly(96) toward the inhibitor molecule. We conclude that the decreased inhibitory potency observed for glyphosate is a result of these mutation-induced long-range structural changes. The implications of our findings concerning the development and spread of glyphosate-resistant weeds are discussed.
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(as it appears on PubMed at http://www.pubmed.gov), where 17855366 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17855366}}
==About this Structure==
==About this Structure==
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[[Category: Inside-out alpha-beta barrel]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:52:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:41:34 2008''

Revision as of 16:41, 28 July 2008

Image:2qfq.png

Template:STRUCTURE 2qfq

E. coli EPSP synthase Pro101Leu liganded with S3P

Template:ABSTRACT PUBMED 17855366

About this Structure

2QFQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase., Healy-Fried ML, Funke T, Priestman MA, Han H, Schonbrunn E, J Biol Chem. 2007 Nov 9;282(45):32949-55. Epub 2007 Sep 12. PMID:17855366

Page seeded by OCA on Mon Jul 28 19:41:34 2008

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