› 3k52

X-ray diffraction
2.7Å resolution

Crystal Structure of Isopentenyl Phosphate Kinase from M. jannaschii in complex with IP

Released:
DOI: 10.2210/pdb3k52/pdb
PDB entry 3k52 coloured by chain, front view.
PDB entry 3k52 coloured by chain, side view.
PDB entry 3k52 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
Mutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates.
Dellas N, Noel JP
ACS Chem Biol 5 589-601 (2010)
PMID: 20392112

Function and Biology Details

Reaction catalysed: 
ATP + 3-methylbut-3-en-1-yl phosphate = ADP + 3-methylbut-3-en-1-yl diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-178768 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isopentenyl phosphate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 30.01 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q60352 (Residues: 1-260; Coverage: 100%)
Gene name: MJ0044
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

2 bound ligands:
Ligand IP8 2 x IP8
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21212
Unit cell:
a: 77.86Å b: 100.8Å c: 87.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.224 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko HM. (2011)
5 more

1 mention without citation

Mutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates.
Dellas et al. (2010)