› 7v4o

X-ray diffraction
1.65Å resolution

Unique non-heme hydroxylase in biosynthesis of nucleoside antibiotic pathway uncover mechanism of reaction

Released:
DOI: 10.2210/pdb7v4o/pdb
PDB entry 7v4o coloured by chain, front view.
PDB entry 7v4o coloured by chain, side view.
PDB entry 7v4o coloured by chain, top view.
Source organism: Streptomyces sp. MK730-62F2
Primary publication:
beta-Hydroxylation of alpha-amino-beta-hydroxylbutanoyl-glycyluridine catalyzed by a nonheme hydroxylase ensures the maturation of caprazamycin
Zadeh SM, Chen MH, Wang ZC, Astani EK, Lo IW, Lin KH, Hsu NS, Adhikari K, Lyu SY, Tsai HY, Terasawa Y, Yabe M, Yamamoto K, Ichikawa S, Li TL
Commun Chem 5 87- (2022)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111359 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartyl/asparaginy/proline hydroxylase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 182 amino acids
Theoretical weight: 21 KDa
Source organism: Streptomyces sp. MK730-62F2
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpGUT1
UniProt:
  • Canonical: C4NCJ7 (Residues: 1-182; Coverage: 100%)
Gene name: cpz10
Sequence domains: Aspartyl/Asparaginyl beta-hydroxylase

Ligands and Environments

1 bound ligand:
Ligand P3G 2 x P3G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE TPS 05A
Spacegroup: C2
Unit cell:
a: 150.839Å b: 39.035Å c: 76.591Å
α: 90° β: 119.34° γ: 90°
R-values:
R R work R free
0.182 0.18 0.214
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpGUT1

Quick links

Citations

1 citations in other articles

Carbon-nitrogen bond formation to construct novel polyketide-indole hybrids from the indole-3-carbinol exposed culture of Daldinia eschscholzii.
Lin et al. (2022)