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EPSP synthase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='1g6s' size='350' side='right' caption='Structure of EPSP synthase (PDB entry [[ | + | <StructureSection load='1g6s' size='350' side='right' caption='Structure of E. coli EPSP synthase complex with shikimate-3-phosphate, the herbicide glyphosate and formic acid (PDB entry [[1g6s]])' scene=''> |
== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
| - | EPSP synthase is a target for drugs and herbicides. | + | EPSP synthase is a target for drugs and herbicides like '''Roundup'''. |
== Structural insights == | == Structural insights == | ||
| - | The enzyme has <scene name='57/570585/Two_domains/1'>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/1'>closed formation</scene>. '''Glyphosate''' (also known as '''Roundup''') occupies the binding site of the second substrate, phosphoenol pyruvate. | + | The enzyme has <scene name='57/570585/Two_domains/1'>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/1'>closed formation</scene>. '''Glyphosate''' (also known as '''Roundup''') occupies the binding site of the second substrate, phosphoenol pyruvate <ref>PMID:11171958</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 21:51, 19 January 2016
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3D structures of EPSP synthase
Updated on 19-January-2016
References
- ↑ 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
- ↑ 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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