› 3pqb

X-ray diffraction
2.32Å resolution

The crystal structure of pregilvocarcin in complex with GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis

Released:
DOI: 10.2210/pdb3pqb/pdb
PDB entry 3pqb coloured by chain, front view.
PDB entry 3pqb coloured by chain, side view.
PDB entry 3pqb coloured by chain, top view.
Source organism: Streptomyces griseoflavus
Primary publication:
The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis.
Noinaj N, Bosserman MA, Schickli MA, Piszczek G, Kharel MK, Pahari P, Buchanan SK, Rohr J
J Biol Chem 286 23533-43 (2011)
PMID: 21561854

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-binding PCMH-type domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 501 amino acids
Theoretical weight: 54.41 KDa
Source organism: Streptomyces griseoflavus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7X2G7 (Residues: 1-498; Coverage: 100%)
Gene name: gilR
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FAD 4 x FAD
Ligand VGP 4 x VGP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 68.003Å b: 115.973Å c: 291.405Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.205
Expression system: Escherichia coli

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Citations

3 review citations

Delineation of gilvocarcin, jadomycin, and landomycin pathways through combinatorial biosynthetic enzymology.
Kharel et al. (2012)
2 more

1 mention without citation

The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis.
Noinaj et al. (2011)