› 1rf4

X-ray diffraction
2.2Å resolution

Structural Studies of Streptococcus pneumoniae EPSP Synthase, Tetrahedral intermediate Bound State

Released:
DOI: 10.2210/pdb1rf4/pdb
PDB entry 1rf4 coloured by chain, front view.
PDB entry 1rf4 coloured by chain, side view.
PDB entry 1rf4 coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate-bound state and S3P-GLP-bound state.
Park H, Hilsenbeck JL, Kim HJ, Shuttleworth WA, Park YH, Evans JN, Kang C
Mol Microbiol 51 963-71 (2004)
PMID: 14763973

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-193392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-phosphoshikimate 1-carboxyvinyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 427 amino acids
Theoretical weight: 45.88 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9S400 (Residues: 1-427; Coverage: 100%)
Gene names: SP_1371, aroA
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

1 bound ligand:
Ligand SPQ 4 x SPQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 82.495Å b: 149.705Å c: 88.011Å
α: 90° β: 91.22° γ: 90°
R-values:
R R work R free
0.243 0.196 0.236
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Molecular basis of glyphosate resistance-different approaches through protein engineering.
Pollegioni et al. (2011)
16 other articles

3 mentions without citation

Coevolutionary signals across protein lineages help capture multiple protein conformations.
Morcos et al. (2013)
2 more