› 5ckv

X-ray diffraction
2.79Å resolution

DAHP synthase from Mycobacterium tuberculosis, fully inhibited by tyrosine, phenylalanine, and tryptophan

Released:
DOI: 10.2210/pdb5ckv/pdb
Model geometry
Fit model/data
PDB entry 5ckv coloured by chain, front view.
PDB entry 5ckv coloured by chain, side view.
PDB entry 5ckv coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Remote Control by Inter-Enzyme Allostery: A Novel Paradigm for Regulation of the Shikimate Pathway.
Munack S, Roderer K, Ökvist M, Kamarauskaite J, Sasso S, van Eerde A, Kast P, Krengel U
J Mol Biol 428 1237-1255 (2016)
PMID: 26776476

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129443 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospho-2-dehydro-3-deoxyheptonate aldolase AroG Chains: A, B
Molecule details ›
Chains: A, B
Length: 472 amino acids
Theoretical weight: 51.89 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O53512 (Residues: 1-462; Coverage: 100%)
Gene names: Rv2178c, aroG
Sequence domains: Class-II DAHP synthetase family

Ligands and Environments

7 bound ligands:
Ligand CL 2 x CL
Ligand SO4 5 x SO4
Ligand GOL 5 x GOL
Ligand TRP 2 x TRP
Ligand MN 2 x MN
Ligand PHE 2 x PHE
Ligand TYR 1 x TYR
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 204.76Å b: 204.76Å c: 66.774Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.175 0.226
Expression system: Escherichia coli

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Citations

5 review citations

Spatial Organization of Metabolic Enzyme Complexes in Cells.
Schmitt et al. (2017)
4 more

1 mention without citation

Quaternary structure is an essential component that contributes to the sophisticated allosteric regulation mechanism in a key enzyme from Mycobacterium tuberculosis.
Jiao et al. (2017)