› 1se6

X-ray diffraction
1.75Å resolution

Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathways

Released:
DOI: 10.2210/pdb1se6/pdb
PDB entry 1se6 coloured by chain, front view.
PDB entry 1se6 coloured by chain, side view.
PDB entry 1se6 coloured by chain, top view.
Source organism: Streptomyces coelicolor A3(2)
Primary publication:
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2.
Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR
J Biol Chem 280 11599-607 (2005)
PMID: 15659395

Function and Biology Details

Reaction catalysed: 
2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,3'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190285 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biflaviolin synthase CYP158A2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 44.68 KDa
Source organism: Streptomyces coelicolor A3(2)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FCA6 (Residues: 1-404; Coverage: 100%)
Gene names: SCO1207, cyp158a2
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

3 bound ligands:
Ligand SPK 1 x SPK
Ligand HEM 2 x HEM
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 59.554Å b: 79.206Å c: 87.43Å
α: 90° β: 92.26° γ: 90°
R-values:
R R work R free
0.234 0.234 0.268
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Cytochromes P450 as versatile biocatalysts.
Bernhardt R. (2006)
26 more

5 mentions without citation

Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.
Rudolf et al. (2017)
4 more