› 2x9o

X-ray diffraction
1.55Å resolution

STRUCTURE OF 15, 16- DIHYDROBILIVERDIN:FERREDOXIN OXIDOREDUCTASE (PebA)

Released:
DOI: 10.2210/pdb2x9o/pdb
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Source organism: Synechococcus sp. WH 8020
Primary publication:
Structural and mechanistic insight into the ferredoxin-mediated two-electron reduction of bilins.
Busch AW, Reijerse EJ, Lubitz W, Frankenberg-Dinkel N, Hofmann E
Biochem J 439 257-64 (2011)
PMID: 21729003

Function and Biology Details

Reaction catalysed: 
15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IX-alpha + reduced ferredoxin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
15,16-dihydrobiliverdin:ferredoxin oxidoreductase Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 28.14 KDa
Source organism: Synechococcus sp. WH 8020
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02189 (Residues: 2-236; Coverage: 100%)
Gene name: pebA
Sequence domains: Ferredoxin-dependent bilin reductase
Structure domains: oxygen-dependent coproporphyrinogen oxidase

Ligands and Environments

1 bound ligand:
Ligand BLA 1 x BLA
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 42.42Å b: 39.35Å c: 71.27Å
α: 90° β: 105.64° γ: 90°
R-values:
R R work R free
0.181 0.179 0.225
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Plant type ferredoxins and ferredoxin-dependent metabolism.
Hanke et al. (2013)
10 other articles

2 mentions without citation

Ferredoxin-dependent bilin reductases in eukaryotic algae: Ubiquity and diversity.
Rockwell et al. (2017)
1 more

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