PDBsum entry 1g6t

Transferase

PDB id: 1g6t

Contents

Protein chain

427 a.a. *

Ligands

PO4

S3P

FMT ×13

Waters ×555

* Residue conservation analysis

PDB id:

1g6t

Name:

Transferase

Title:

Structure of epsp synthase liganded with shikimate-3-phosphate

Structure:

Epsp synthase. Chain: a. Synonym: 3-phosphoshikimate 1-carboxyvinyltransferase. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: aroa. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.60Å R-factor: 0.155 R-free: 0.185

Authors:

E.Schonbrunn,S.Eschenburg,W.Shuttleworth,J.V.Schloss,N.Amrhein, J.N.S.Evans,W.Kabsch

Key ref:

E.Schönbrunn et al. (2001). Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci U S A, 98, 1376-1380. PubMed id: 11171958 DOI: 10.1073/pnas.98.4.1376

Date:

07-Nov-00 Release date: 07-Feb-01

Protein chain

P0A6D3  (AROA_ECOLI) -  3-phosphoshikimate 1-carboxyvinyltransferase from Escherichia coli (strain K12)

Seq: 427 a.a.

Struc: 427 a.a.

Enzyme reactions

• Enzyme class: E.C.2.5.1.19 - 3-phosphoshikimate 1-carboxyvinyltransferase.
• Pathway: Shikimate and Chorismate Biosynthesis
• Reaction: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3- phosphoshikimate + phosphate

3-phosphoshikimate + phosphoenolpyruvate (Bound ligand (Het Group name = S3P) matches with 52.94% similarity) = 5-O-(1-carboxyvinyl)-3- phosphoshikimate + phosphate (Bound ligand (Het Group name = PO4) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1073/pnas.98.4.1376

Proc Natl Acad Sci U S A 98:1376-1380 (2001)

PubMed id: 11171958

Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail.

E.Schönbrunn, S.Eschenburg, W.A.Shuttleworth, J.V.Schloss, N.Amrhein, J.N.Evans, W.Kabsch.

ABSTRACT

Biosynthesis of aromatic amino acids in plants, many bacteria, and microbes relies on the enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase, a prime target for drugs and herbicides. We have identified the interaction of EPSP synthase with one of its two substrates (shikimate 3-phosphate) and with the widely used herbicide glyphosate by x-ray crystallography. The two-domain enzyme closes on ligand binding, thereby forming the active site in the interdomain cleft. Glyphosate appears to occupy the binding site of the second substrate of EPSP synthase (phosphoenol pyruvate), mimicking an intermediate state of the ternary enzyme.substrates complex. The elucidation of the active site of EPSP synthase and especially of the binding pattern of glyphosate provides a valuable roadmap for engineering new herbicides and herbicide-resistant crops, as well as new antibiotic and antiparasitic drugs.

Selected figure(s)

Figure 1.
Fig. 1. Cartoon of EPSP synthase in the open and closed conformation. Top domain, residues 20-240; bottom domain, residues 1-19 plus 241-427. (a) Unliganded state (open) as reconstructed from the deposited -carbon atoms (Protein Data Bank entry code 1EPS). (b) Liganded state (closed). S3P and glyphosate are shown as ball-and-stick models in green and magenta, respectively. Drawn with BOBSCRIPT (24).

Figure 3.
Fig. 3. Schematic representation of ligand binding in the EPSP synthase·S3P·glyphosate complex. Ligands are drawn in bold lines. Dashed lines indicate hydrogen bonds and ionic interactions. Strictly conserved residues are highlighted by bold labels. Protein atoms are labeled according to the Protein Data Bank nomenclature. Circled labels W1 to W4 designate solvent molecules. Hydrophobic interactions between S3P and Tyr-200 are omitted.

Figures were selected by an automated process.