› 5ve4

X-ray diffraction
2.65Å resolution

Crystal structure of persulfide dioxygenase-rhodanese fusion protein with rhodanese domain inactivating mutation (C314S) from Burkholderia phytofirmans

Released:
DOI: 10.2210/pdb5ve4/pdb
PDB entry 5ve4 coloured by chain, front view.
PDB entry 5ve4 coloured by chain, side view.
PDB entry 5ve4 coloured by chain, top view.
Source organism: Paraburkholderia phytofirmans PsJN
Primary publication:
Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.
Motl N, Skiba MA, Kabil O, Smith JL, Banerjee R
J Biol Chem 292 14026-14038 (2017)
PMID: 28684420

Function and Biology Details

Reactions catalysed: 
(1a) S-sulfanylglutathione + O(2) = glutathione S-dioxide + H(+)
Thiosulfate + cyanide = sulfite + thiocyanate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-502525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhodanese domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 377 amino acids
Theoretical weight: 41.6 KDa
Source organism: Paraburkholderia phytofirmans PsJN
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B2TEQ2 (Residues: 1-357; Coverage: 100%)
Gene name: Bphyt_4191
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand FE 3 x FE
Ligand CL 3 x CL
Ligand PEG 1 x PEG
Ligand GOL 1 x GOL
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P6522
Unit cell:
a: 84.504Å b: 84.504Å c: 549.379Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.232 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

H2S and reactive sulfur signaling at the host-bacterial pathogen interface.
Walsh et al. (2020)
4 more

1 mention without citation

Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.
Motl et al. (2017)