EPSP synthase: Difference between revisions

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== Structural insights ==
== Structural insights ==


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  of the second substrate, phosphoenol pyruvate <ref>PMID:11171958</ref>.  Interestingly CP4 EPSP synthase still binds glyphosate in the absence of PEP, but a conformational change in glyphosate to accomodate a steric clash with <scene name='57/570585/Glyphosate_s3p_distance/2'>Glu 354</scene> shortens the length of glyphosate, from 7.3 angstroms to 6.67 angstroms, and changes the IC50 by a factor of over 4,000, from 2.5 micromolar to 11 millimolar.   
The enzyme has two domains, with the active site found in the interdomain cleft <scene name='57/570585/Two_domains/4'>(open conformation)</scene>.  There is a substantial structural change upon substrate binding, resulting in a <scene name='57/570585/Closed_formation/3'>closed</scene> conformation. <scene name='57/570585/Cv/9'>See animation of this process</scene>. '''Glyphosate''' (also known as '''Roundup''') occupies the  of the second substrate, phosphoenol pyruvate <ref>PMID:11171958</ref>.  Interestingly CP4 EPSP synthase still binds glyphosate in the absence of PEP, but a conformational change in glyphosate to accomodate a steric clash with <scene name='57/570585/Glyphosate_s3p_distance/2'>Glu 354</scene> shortens the length of glyphosate, from 7.3 angstroms to 6.67 angstroms, and changes the IC50 by a factor of over 4,000, from 2.5 micromolar to 11 millimolar.   
</StructureSection>
</StructureSection>


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Ann Taylor, Michal Harel, Alexander Berchansky, Joel L. Sussman