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| <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='57/570585/Cv/1'> | | <StructureSection load='1g6s' size='450' side='right' caption='Structure of E. coli EPSP synthase complex with shikimate-3-phosphate, the herbicide glyphosate and formic acid (PDB entry [[1g6s]])' scene='57/570585/Cv/1'> |
| == Function == | | == Function == |
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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 binding site of the second substrate, phosphoenol pyruvate <ref>PMID:11171958</ref>. | | 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>. |
| </StructureSection> | | </StructureSection> |
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Revision as of 15:52, 20 January 2016
| Function
5-enolpyruvylshikimate 3-phosphate (EPSP) synthase is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. Consequently. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate (S3P), generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine[1].
Relevance
EPSP synthase is a target for drugs and herbicides like Roundup.
Structural insights
The enzyme has two domains, with the active site found in the interdomain cleft. There is a substantial structural change upon substrate binding, resulting in a closed formation. See animation of this process. Glyphosate (also known as Roundup) occupies the binding site of the second substrate, phosphoenol pyruvate [2].
- ↑ 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:https://dx.doi.org/10.1073/pnas.98.4.1376
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3D structures of EPSP synthase
Updated on 20-January-2016
{"openlevels":0}
- 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase
- 1eps – EcEPSP – Escherichia coli
- 1p88, 1p89 - EcEPSP N terminal - NMR
- 1rf5 - SpEPSP – Streptococcus pneumoniae
- 2bjb, 2o15 – MtEPSP – Mycobacterium tuberculosis
- 2gg4 – AgEPSP – Agrobacterium
- 3roi, 3tr1, 4gfp – CbEPSP – Coxiella burnetii
- 3ti2 - VcEPSP N terminal – Vibrio cholerae
- 3rmt – EPSP – Bacillus halodurans
- EPSP synthase binary complex
- EPSP synthase ternary complex
- 1g6s - EcEPSP + S3P + glyphosate
- 2qft, 2qfu, 3fjz, 3fk1 - EcEPSP (mutant) + S3P + glyphosate
- 2aay - EcEPSP + shikimate + glyphosate
- 1rf6 - SpEPSP + S3P + glyphosate
- 2gga - AgEPSP + S3P + glyphosate
- 2ggd - AgEPSP (mutant) + S3P + glyphosate
- 2o0e - MtEPSP + S3P + phosphoenolpyruvate
- 3nvs - VcEPSP + S3P + glyphosate
- 3slh - CbEPSP + S3P + glyphosate
References
