2aay

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(New page: 200px<br /><applet load="2aay" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aay, resolution 1.55&Aring;" /> '''EPSP synthase ligand...)
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[[Image:2aay.gif|left|200px]]<br /><applet load="2aay" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2aay, resolution 1.55&Aring;" />
caption="2aay, resolution 1.55&Aring;" />
'''EPSP synthase liganded with shikimate and glyphosate'''<br />
'''EPSP synthase liganded with shikimate and glyphosate'''<br />
==Overview==
==Overview==
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The shikimate pathway enzyme 5-enolpyruvyl shikimate-3-phosphate synthase, (EPSP synthase) has received attention in the past because it is the, target of the broad-spectrum herbicide glyphosate. The natural substrate, of EPSP synthase is shikimate-3-phosphate. However, this enzyme can also, utilize shikimate as substrate. Remarkably, this reaction is insensitive, to inhibition by glyphosate. Crystallographic analysis of EPSP synthase, from Escherichia coli, in complex with shikimate/glyphosate at 1.5, Angstroms resolution, revealed that binding of shikimate induces changes, around the backbone of the active site, which in turn impact the efficient, binding of glyphosate. The implications from these findings with respect, to the design of novel glyphosate-insensitive EPSP synthase enzymes are, discussed.
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The shikimate pathway enzyme 5-enolpyruvyl shikimate-3-phosphate synthase (EPSP synthase) has received attention in the past because it is the target of the broad-spectrum herbicide glyphosate. The natural substrate of EPSP synthase is shikimate-3-phosphate. However, this enzyme can also utilize shikimate as substrate. Remarkably, this reaction is insensitive to inhibition by glyphosate. Crystallographic analysis of EPSP synthase from Escherichia coli, in complex with shikimate/glyphosate at 1.5 Angstroms resolution, revealed that binding of shikimate induces changes around the backbone of the active site, which in turn impact the efficient binding of glyphosate. The implications from these findings with respect to the design of novel glyphosate-insensitive EPSP synthase enzymes are discussed.
==About this Structure==
==About this Structure==
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2AAY 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 SKM, GPJ 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=2AAY OCA].
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2AAY 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=SKM:'>SKM</scene>, <scene name='pdbligand=GPJ:'>GPJ</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=2AAY OCA].
==Reference==
==Reference==
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[[Category: Becker, A.]]
[[Category: Becker, A.]]
[[Category: Funke, T.]]
[[Category: Funke, T.]]
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[[Category: Healy, M.L.]]
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[[Category: Healy, M L.]]
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[[Category: Priestman, M.A.]]
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[[Category: Priestman, M A.]]
[[Category: FMT]]
[[Category: FMT]]
[[Category: GPJ]]
[[Category: GPJ]]
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[[Category: inside-out alpha/beta barrel]]
[[Category: inside-out alpha/beta barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:01:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:36 2008''

Revision as of 14:25, 21 February 2008


2aay, resolution 1.55Å

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EPSP synthase liganded with shikimate and glyphosate

Overview

The shikimate pathway enzyme 5-enolpyruvyl shikimate-3-phosphate synthase (EPSP synthase) has received attention in the past because it is the target of the broad-spectrum herbicide glyphosate. The natural substrate of EPSP synthase is shikimate-3-phosphate. However, this enzyme can also utilize shikimate as substrate. Remarkably, this reaction is insensitive to inhibition by glyphosate. Crystallographic analysis of EPSP synthase from Escherichia coli, in complex with shikimate/glyphosate at 1.5 Angstroms resolution, revealed that binding of shikimate induces changes around the backbone of the active site, which in turn impact the efficient binding of glyphosate. The implications from these findings with respect to the design of novel glyphosate-insensitive EPSP synthase enzymes are discussed.

About this Structure

2AAY 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.

Reference

Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate., Priestman MA, Healy ML, Funke T, Becker A, Schonbrunn E, FEBS Lett. 2005 Oct 24;579(25):5773-80. PMID:16225867

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