› 2qmw

X-ray diffraction
2.3Å resolution

The crystal structure of the prephenate dehydratase (PDT) from Staphylococcus aureus subsp. aureus Mu50

Released:
DOI: 10.2210/pdb2qmw/pdb
PDB entry 2qmw coloured by chain, front view.
PDB entry 2qmw coloured by chain, side view.
PDB entry 2qmw coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus Mu50
Primary publication:
Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine.
Tan K, Li H, Zhang R, Gu M, Clancy ST, Joachimiak A
J Struct Biol 162 94-107 (2008)
PMID: 18171624

Function and Biology Details

Reaction catalysed: 
Prephenate = phenylpyruvate + H(2)O + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102018 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
prephenate dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 30 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A0H3K044 (Residues: 1-264; Coverage: 100%)
Gene name: SAV1915
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand NA 1 x NA
Ligand ACT 1 x ACT
Ligand EDO 2 x EDO
Ligand PEG 1 x PEG
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21212
Unit cell:
a: 60.859Å b: 87.406Å c: 107.744Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.225 0.276
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism.
Lang et al. (2014)
1 more

2 mentions without citation

Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine.
Tan et al. (2008)
1 more