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EPSP synthase

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== Structural insights ==
== Structural insights ==
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The enzyme has <scene name='57/570585/Two_domains/2'>two domains</scene>, with the active site found in the interdomain cleft. There is a substantial structural change upon substrate binding, resulting in a <scene name='57/570585/Closed_formation/2'>closed formation</scene>. <scene name='57/570585/Cv/3'>See animation of this process</scene>. '''Glyphosate''' (also known as '''Roundup''') occupies the <scene name='57/570585/Cv/8'>binding site</scene> of the second substrate, phosphoenol pyruvate <ref>PMID:11171958</ref>.
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The enzyme has two domains, with the active site found in the interdomain cleft <scene name='57/570585/Two_domains/2'>(open conformation)</scene>. There is a substantial structural change upon substrate binding, resulting in a <scene name='57/570585/Closed_formation/2'>closed</scene> conformation. <scene name='57/570585/Cv/3'>See animation of this process</scene>. '''Glyphosate''' (also known as '''Roundup''') occupies the <scene name='57/570585/Cv/8'>binding site</scene> of the second substrate, phosphoenol pyruvate <ref>PMID:11171958</ref>.
</StructureSection>
</StructureSection>

Revision as of 15:54, 20 January 2016

Structure of E. coli EPSP synthase complex with shikimate-3-phosphate, the herbicide glyphosate and formic acid (PDB entry 1g6s)

Drag the structure with the mouse to rotate

3D structures of EPSP synthase

Updated on 20-January-2016

References

  1. Priestman MA, Healy ML, Funke T, Becker A, Schonbrunn E. Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate. FEBS Lett. 2005 Oct 24;579(25):5773-80. PMID:16225867 doi:10.1016/j.febslet.2005.09.066
  2. Schonbrunn E, Eschenburg S, Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1376-80. PMID:11171958 doi:http://dx.doi.org/10.1073/pnas.98.4.1376

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