› 2aa9

X-ray diffraction
1.5Å resolution

EPSP synthase liganded with shikimate

Released:
DOI: 10.2210/pdb2aa9/pdb
PDB entry 2aa9 coloured by chain, front view.
PDB entry 2aa9 coloured by chain, side view.
PDB entry 2aa9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate.
Priestman MA, Healy ML, Funke T, Becker A, Schönbrunn E
FEBS Lett 579 5773-80 (2005)
PMID: 16225867

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-531792 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-phosphoshikimate 1-carboxyvinyltransferase Chain: A
Molecule details ›
Chain: A
Length: 427 amino acids
Theoretical weight: 46.14 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6D3 (Residues: 1-427; Coverage: 100%)
Gene names: JW0891, aroA, b0908
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

2 bound ligands:
Ligand SKM 1 x SKM
Ligand FMT 17 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 58.075Å b: 85.025Å c: 87.633Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 0.183
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

A novel 5-enolpyruvylshikimate-3-phosphate synthase shows high glyphosate tolerance in Escherichia coli and tobacco plants.
Cao et al. (2012)
7 more

1 mention without citation

An Evolutionary Conservation and Druggability Analysis of Enzymes Belonging to the Bacterial Shikimate Pathway.
Frlan R. (2022)