Structure of EPSP Synthase
|
5-enolpyruvylshikimate 3-phosphate (EPSP) synthase is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. Consequently, it is a target for drugs and herbicides. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate, generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine.
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. Glyphosate (also known as Roundup) occupies the binding site of the second substrate, phosphoenol pyruvate.
|
3D structures of EPSP synthase
Updated on 24-November-2014
{"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
- EPSP synthase binary complex
- EPSP synthase ternary complex
- 1g6p - EcEPSP + S3P + glyphosate
- 2qft, 2qfu, 3fjz, 3fk1 - EcEPSP (mutant) + S3P + glyphosate
- 2aay - EcEPSP + shikimate + glyphosate
- 1rf6 - SpEPSP + S3P + glyphosate
- 2gga - AgEPSP + S3P + glyphosate
- 4ggd - AgEPSP (mutant) + S3P + glyphosate
- 2o0e - MtEPSP + S3P + phosphoenolpyruvate
- 3nvs - VcEPSP + S3P + glyphosate
- 3slh - CbEPSP + S3P + glyphosate
