› 1r30

X-ray diffraction
3.4Å resolution

The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme

Released:
DOI: 10.2210/pdb1r30/pdb
PDB entry 1r30 coloured by chain, front view.
PDB entry 1r30 coloured by chain, side view.
PDB entry 1r30 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme.
Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL
Science 303 76-9 (2004)
PMID: 14704425

Function and Biology Details

Reaction catalysed: 
Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146422 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biotin synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 369 amino acids
Theoretical weight: 41.36 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P12996 (Residues: 2-346; Coverage: 100%)
Gene names: JW0758, b0775, bioB
Sequence domains:
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand SAM 2 x SAM
4 bound ligands:
Ligand SF4 2 x SF4
Ligand FES 2 x FES
Ligand DTB 2 x DTB
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3121
Unit cell:
a: 155.69Å b: 155.69Å c: 90.88Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.256 0.256 0.3
Expression system: Escherichia coli

Quick links

Citations

56 review citations

Structure, function, and formation of biological iron-sulfur clusters.
Johnson et al. (2005)
55 more

32 mentions without citation

Radical S-adenosylmethionine enzymes.
Broderick et al. (2014)
31 more