› 7cpm

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF DODECAPRENYL DIPHOSPHATE SYNTHASE FROM THERMOBIFIDA FUSCA

Released:
DOI: 10.2210/pdb7cpm/pdb
PDB entry 7cpm coloured by chain, front view.
PDB entry 7cpm coloured by chain, side view.
PDB entry 7cpm coloured by chain, top view.
Source organism: Thermobifida fusca YX
Primary publication:
Crystal structure of Thermobifida fusca cis-prenyltransferase reveals the dynamic nature of its RXG motif-mediated inter-subunit interactions critical for its catalytic activity.
Kurokawa H, Ambo T, Takahashi S, Koyama T
Biochem Biophys Res Commun 532 459-465 (2020)
PMID: 32892948

Function and Biology Details

Reaction catalysed: 
(2Z,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + trans,polycis-polyprenyl diphosphate (n = 9-11)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175314 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trans,polycis-polyprenyl diphosphate synthase ((2Z,6E)-farnesyl diphosphate specific) Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 288 amino acids
Theoretical weight: 32.65 KDa
Source organism: Thermobifida fusca YX
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47RM6 (Residues: 1-282; Coverage: 100%)
Gene name: Tfu_0853
Sequence domains: Putative undecaprenyl diphosphate synthase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 70.862Å b: 137.59Å c: 168.854Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.234
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Reconstitution of prenyltransferase activity on nanodiscs by components of the rubber synthesis machinery of the Para rubber tree and guayule.
Kuroiwa et al. (2022)