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X-ray diffraction
3.1Å resolution

Structural and Mechanistic Analysis of the Magnesium-Independent Aromatic Prenyltransferase CloQ from the Clorobiocin Biosynthetic Pathway

Released:
DOI: 10.2210/pdb2xly/pdb
PDB entry 2xly coloured by chain, front view.
PDB entry 2xly coloured by chain, side view.
PDB entry 2xly coloured by chain, top view.
Source organism: Streptomyces roseochromogenus subsp. oscitans
Primary publication:
Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway.
Metzger U, Keller S, Stevenson CE, Heide L, Lawson DM
J Mol Biol 404 611-26 (2010)
PMID: 20946900

Function and Biology Details

Reaction catalysed: 
Prenyl diphosphate + 3-(4-hydroxyphenyl)pyruvate = diphosphate + 3-(4-hydroxy-3-prenylphenyl)pyruvate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxyphenylpyruvate 3-dimethylallyltransferase Chain: A
Molecule details ›
Chain: A
Length: 327 amino acids
Theoretical weight: 35.95 KDa
Source organism: Streptomyces roseochromogenus subsp. oscitans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8GHB2 (Residues: 1-324; Coverage: 100%)
Gene name: cloQ
Sequence domains: Aromatic prenyltransferase Orf2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I4122
Unit cell:
a: 135.57Å b: 135.57Å c: 95.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.236
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

Terpenoid synthase structures: a so far incomplete view of complex catalysis.
Gao et al. (2012)
6 more