1g6t: Difference between revisions

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New page: left|200px<br /><applet load="1g6t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g6t, resolution 1.60Å" /> '''STRUCTURE OF EPSP SY...
 
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[[Image:1g6t.jpg|left|200px]]<br /><applet load="1g6t" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g6t, resolution 1.60&Aring;" />
caption="1g6t, resolution 1.60&Aring;" />
'''STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE'''<br />
'''STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1G6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, S3P and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-phosphoshikimate_1-carboxyvinyltransferase 3-phosphoshikimate 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.19 2.5.1.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G6T OCA].  
1G6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=S3P:'>S3P</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3-phosphoshikimate_1-carboxyvinyltransferase 3-phosphoshikimate 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.19 2.5.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6T OCA].  


==Reference==
==Reference==
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[[Category: Amrhein, N.]]
[[Category: Amrhein, N.]]
[[Category: Eschenburg, S.]]
[[Category: Eschenburg, S.]]
[[Category: Evans, J.N.S.]]
[[Category: Evans, J N.S.]]
[[Category: Kabsch, W.]]
[[Category: Kabsch, W.]]
[[Category: Schloss, J.V.]]
[[Category: Schloss, J V.]]
[[Category: Schonbrunn, E.]]
[[Category: Schonbrunn, E.]]
[[Category: Shuttleworth, W.]]
[[Category: Shuttleworth, W.]]
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[[Category: two-domain structure; inside-out alpha-beta barrel]]
[[Category: two-domain structure; inside-out alpha-beta barrel]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:45:53 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:45 2008''

Revision as of 13:46, 21 February 2008

File:1g6t.jpg


1g6t, resolution 1.60Å

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STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE

OverviewOverview

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.

About this StructureAbout this Structure

1G6T is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as 3-phosphoshikimate 1-carboxyvinyltransferase, with EC number 2.5.1.19 Full crystallographic information is available from OCA.

ReferenceReference

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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