› 1n8f

X-ray diffraction
1.75Å resolution

Crystal structure of E24Q mutant of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (DAHP synthase) from Escherichia Coli in complex with Mn2+ and PEP

Released:
DOI: 10.2210/pdb1n8f/pdb
PDB entry 1n8f coloured by chain, front view.
PDB entry 1n8f coloured by chain, side view.
PDB entry 1n8f coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The high-resolution structure of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase reveals a twist in the plane of bound phosphoenolpyruvate.
Shumilin IA, Bauerle R, Kretsinger RH
Biochemistry 42 3766-76 (2003)
PMID: 12667068

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 350 amino acids
Theoretical weight: 38.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB91 (Residues: 1-350; Coverage: 100%)
Gene names: JW0737, aroG, b0754
Sequence domains: DAHP synthetase I family
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand MN 4 x MN
Ligand SO4 8 x SO4
Ligand PEP 4 x PEP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 213.224Å b: 53.277Å c: 150.245Å
α: 90° β: 116.9° γ: 90°
R-values:
R R work R free
0.209 0.209 0.237
Expression system: Escherichia coli

Quick links

Citations

18 citation in other articles

The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes.
Webby et al. (2005)
17 more

3 mentions without citation

Anatomy of enzyme channels.
Pravda et al. (2014)
2 more