› 3lgz

X-ray diffraction
2.41Å resolution

Crystal structure of dehydrosqualene synthase Y129A from S. aureus complexed with presqualene pyrophosphate

Released:
DOI: 10.2210/pdb3lgz/pdb
PDB entry 3lgz coloured by chain, front view.
PDB entry 3lgz coloured by chain, side view.
PDB entry 3lgz coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Mechanism of action and inhibition of dehydrosqualene synthase.
Lin FY, Liu CI, Liu YL, Zhang Y, Wang K, Jeng WY, Ko TP, Cao R, Wang AH, Oldfield E
Proc Natl Acad Sci U S A 107 21337-42 (2010)
PMID: 21098670

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 Chain: B
Molecule details ›
Chain: 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

2 bound ligands:
Ligand PS7 1 x PS7
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3221
Unit cell:
a: 80.84Å b: 80.84Å c: 91.264Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.203 0.278
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Structural and Chemical Biology of Terpenoid Cyclases.
Christianson DW. (2017)
6 more

2 mentions without citation

Traditional and new influenza vaccines.
Wong et al. (2013)
1 more