› 5guf

X-ray diffraction
2.4Å resolution

Structural insight into an intramembrane enzyme for archaeal membrane lipids biosynthesis

Released:
DOI: 10.2210/pdb5guf/pdb
PDB entry 5guf coloured by chain, front view.
PDB entry 5guf coloured by chain, side view.
PDB entry 5guf coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Structural and mechanistic insights into the biosynthesis of CDP-archaeol in membranes.
Ren S, Caforio A, Yang Q, Sun B, Yu F, Zhu X, Wang J, Dou C, Fu Q, Huang N, Sun Q, Nie C, Qi S, Gong X, He J, Wei Y, Driessen AJ, Cheng W
Cell Res 27 1378-1391 (2017)
PMID: 28961231

Function and Biology Details

Reaction catalysed: 
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195491 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CDP-archaeol synthase Chain: A
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 19.04 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4
UniProt:
  • Canonical: Q9YF05 (Residues: 1-174; Coverage: 100%)
Gene names: APE_0433, carS
Sequence domains: CDP-archaeol synthase

Ligands and Environments

3 bound ligands:
Ligand CTP 1 x CTP
Ligand MG 3 x MG
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: C2221
Unit cell:
a: 56.505Å b: 89.249Å c: 98.876Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.207 0.249
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4

Quick links

Citations

1 review citation

CDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis.
Blunsom et al. (2020)
2 other articles

4 mentions without citation

The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.
de Kok et al. (2022)
3 more