› 5kzl

X-ray diffraction
1.73Å resolution

Structure of Heme Oxygenase from Leptospira interrogans

Released:
DOI: 10.2210/pdb5kzl/pdb
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Source organism: Leptospira interrogans
Primary publication:
Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.
Soldano A, Klinke S, Otero LH, Rivera M, Catalano-Dupuy DL, Ceccarelli EA
OpenAccess logo PLoS One 12 e0182535 (2017)
PMID: 28771589

Function and Biology Details

Reaction catalysed: 
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 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-184434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 24.23 KDa
Source organism: Leptospira interrogans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8EXM2 (Residues: 1-205; Coverage: 91%)
Gene name: LB_186
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER IMUS MICROFOCUS
Spacegroup: P212121
Unit cell:
a: 37.64Å b: 58.79Å c: 86.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.222
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Immune Modulation by Inhibitors of the HO System.
Fernández-Fierro et al. (2020)
1 other article

1 mention without citation

Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.
Soldano et al. (2017)

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