› 7t71

X-ray diffraction
2.19Å resolution

Crystal Structure of Mevalonate 3,5-Bisphosphate Decarboxylase from Picrophilus Torridus

Released:
DOI: 10.2210/pdb7t71/pdb
PDB entry 7t71 coloured by chain, front view.
PDB entry 7t71 coloured by chain, side view.
PDB entry 7t71 coloured by chain, top view.
Source organism: Picrophilus oshimae DSM 9789
Primary publication:
Crystal structure of mevalonate 3,5-bisphosphate decarboxylase reveals insight into the evolution of decarboxylases in the mevalonate metabolic pathways.
Aoki M, Vinokur J, Motoyama K, Ishikawa R, Collazo M, Cascio D, Sawaya MR, Ito T, Bowie JU, Hemmi H
OpenAccess logo J Biol Chem 298 102111 (2022)
PMID: 35690147

Function and Biology Details

Reaction catalysed: 
(R)-3,5-bisphosphomevalonate = isopentenyl phosphate + CO(2) + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179837 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mevalonate 3,5-bisphosphate decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 369 amino acids
Theoretical weight: 42.24 KDa
Source organism: Picrophilus oshimae DSM 9789
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6L1T9 (Residues: 1-349; Coverage: 100%)
Gene name: PTO0478
Sequence domains: Diphosphomevalonate decarboxylase-like N-terminal domain

Ligands and Environments

1 bound ligand:
Ligand OLA 1 x OLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21212
Unit cell:
a: 153.56Å b: 125.49Å c: 52.14Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Advances in the Synthesis and Analysis of Biologically Active Phosphometabolites.
Wohlgemuth R. (2023)
1 other article

1 mention without citation

Crystal structure of mevalonate 3,5-bisphosphate decarboxylase reveals insight into the evolution of decarboxylases in the mevalonate metabolic pathways.
Aoki et al. (2022)