› 4k2x

X-ray diffraction
2.55Å resolution

OxyS anhydrotetracycline hydroxylase from Streptomyces rimosus

Released:
DOI: 10.2210/pdb4k2x/pdb
PDB entry 4k2x coloured by chain, front view.
PDB entry 4k2x coloured by chain, side view.
PDB entry 4k2x coloured by chain, top view.
Source organism: Streptomyces rimosus subsp. rimosus ATCC 10970
Primary publication:
Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis.
Wang P, Bashiri G, Gao X, Sawaya MR, Tang Y
J Am Chem Soc 135 7138-41 (2013)
PMID: 23621493

Function and Biology Details

Reactions catalysed: 
12-dehydrotetracycline + NADPH + O(2) = 5a,11a-dehydrooxytetracycline + NADP(+) + H(2)O
Anhydrotetracycline + NADPH + O(2) = 12-dehydrotetracycline + NADP(+) + H(2)O
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-125864 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
12-dehydrotetracycline 5-monooxygenase/anhydrotetracycline 6-monooxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 523 amino acids
Theoretical weight: 56.71 KDa
Source organism: Streptomyces rimosus subsp. rimosus ATCC 10970
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: L8EUQ6 (Residues: 1-503; Coverage: 100%)
Gene names: SRIM_10936, oxyS
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FAD 2 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 76.06Å b: 115.13Å c: 121.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.
Greening et al. (2016)
8 more

2 mentions without citation

The Structure of the Antibiotic Deactivating, N-hydroxylating Rifampicin Monooxygenase.
Liu et al. (2016)
1 more