› 3uwm

X-ray diffraction
1.8Å resolution

Ec_IspH in complex with 4-oxobutyl diphosphate (1302)

Released:
DOI: 10.2210/pdb3uwm/pdb
PDB entry 3uwm coloured by chain, front view.
PDB entry 3uwm coloured by chain, side view.
PDB entry 3uwm coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Discovery of acetylene hydratase activity of the iron-sulphur protein IspH.
Span I, Wang K, Wang W, Zhang Y, Bacher A, Eisenreich W, Li K, Schulz C, Oldfield E, Groll M
Nat Commun 3 1042 (2012)
PMID: 22948824

Function and Biology Details

Reaction catalysed: 
Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-3-methylbut-2-enyl diphosphate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 324 amino acids
Theoretical weight: 35.79 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P62623 (Residues: 1-316; Coverage: 100%)
Gene names: JW0027, b0029, ispH, lytB, yaaE
Sequence domains: LytB protein
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SF4 2 x SF4
Ligand 0K2 2 x 0K2
Ligand 0JX 2 x 0JX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 70.66Å b: 80.7Å c: 111.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.185 0.268
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Mechanistic aspects of carotenoid biosynthesis.
Moise et al. (2014)
4 more

2 mentions without citation

Mechanistic insights into the reductive dehydroxylation pathway for the biosynthesis of isoprenoids promoted by the IspH enzyme.
Abdel-Azeim et al. (2015)
1 more