› 3krp

X-ray diffraction
2.42Å resolution

Mint heterotetrameric geranyl pyrophosphate synthase in complex with magnesium and GPP

Released:
DOI: 10.2210/pdb3krp/pdb
PDB entry 3krp coloured by chain, front view.
PDB entry 3krp coloured by chain, side view.
PDB entry 3krp coloured by chain, top view.
Source organism: Mentha x piperita
Primary publication:
Structure of a heterotetrameric geranyl pyrophosphate synthase from mint (Mentha piperita) reveals intersubunit regulation.
Chang TH, Hsieh FL, Ko TP, Teng KH, Liang PH, Wang AH
Plant Cell 22 454-67 (2010)
PMID: 20139160

Function and Biology Details

Reaction catalysed: 
Prenyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-193440 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Geranyl pyrophosphate synthase large subunit Chains: A, D
Molecule details ›
Chains: A, D
Length: 295 amino acids
Theoretical weight: 31.95 KDa
Source organism: Mentha x piperita
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SBR3 (Residues: 84-377; Coverage: 78%)
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase
Gpp synthase small subunit Chains: B, C
Molecule details ›
Chains: B, C
Length: 274 amino acids
Theoretical weight: 29.76 KDa
Source organism: Mentha x piperita
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SBR4 (Residues: 49-313; Coverage: 85%)
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

4 bound ligands:
Ligand PPV 1 x PPV
Ligand MG 4 x MG
Ligand EDO 1 x EDO
Ligand GPP 1 x GPP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P212121
Unit cell:
a: 53.26Å b: 109.022Å c: 182.156Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.263 0.223 0.284
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

1 mention without citation

Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation.
Sasaki et al. (2011)