1g6s

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{{STRUCTURE_1g6s| PDB=1g6s | SCENE= }}
{{STRUCTURE_1g6s| PDB=1g6s | SCENE= }}
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'''STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE'''
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===STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11171958 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11171958}}
==About this Structure==
==About this Structure==
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[[Category: Inside-out alpha-beta barrel]]
[[Category: Inside-out alpha-beta barrel]]
[[Category: Two-domain structure]]
[[Category: Two-domain structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:46:08 2008''

Revision as of 01:46, 1 July 2008

Image:1g6s.png

Template:STRUCTURE 1g6s

STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE

Template:ABSTRACT PUBMED 11171958

About this Structure

1G6S is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail., Schonbrunn E, Eschenburg S, Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1376-80. PMID:11171958

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