› 3vje

X-ray diffraction
2.12Å resolution

Crystal structure of the Y248A mutant of C(30) carotenoid dehydrosqualene synthase from Staphylococcus aureus in complex with zaragozic acid A

Released:
DOI: 10.2210/pdb3vje/pdb
PDB entry 3vje coloured by chain, front view.
PDB entry 3vje coloured by chain, side view.
PDB entry 3vje coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Binding modes of zaragozic acid A to human squalene synthase and staphylococcal dehydrosqualene synthase.
Liu CI, Jeng WY, Chang WJ, Ko TP, Wang AH
J Biol Chem 287 18750-7 (2012)
PMID: 22474324

Function and Biology Details

Reaction catalysed: 
(1a) 2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108994 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4,4'-diapophytoene synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 34.7 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: A9JQL9 (Residues: 1-287; Coverage: 100%)
Gene name: crtM
Sequence domains: Squalene/phytoene synthase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

1 bound ligand:
Ligand ZGA 2 x ZGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P3121
Unit cell:
a: 80.177Å b: 80.177Å c: 185.414Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.205 0.254
Expression system: Escherichia coli

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Citations

2 review citations

Human isoprenoid synthase enzymes as therapeutic targets.
Park et al. (2014)
1 more

1 mention without citation

Binding modes of zaragozic acid A to human squalene synthase and staphylococcal dehydrosqualene synthase.
Liu et al. (2012)