› 1cbf

X-ray diffraction
2.4Å resolution

THE X-RAY STRUCTURE OF A COBALAMIN BIOSYNTHETIC ENZYME, COBALT PRECORRIN-4 METHYLTRANSFERASE, CBIF

Released:
DOI: 10.2210/pdb1cbf/pdb
PDB entry 1cbf coloured by chain, front view.
PDB entry 1cbf coloured by chain, side view.
PDB entry 1cbf coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase.
Schubert HL, Wilson KS, Raux E, Woodcock SC, Warren MJ
Nat Struct Biol 5 585-92 (1998)
PMID: 9665173

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + cobalt-precorrin-4 = S-adenosyl-L-homocysteine + cobalt-precorrin-5A
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-131503 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cobalt-precorrin-4 C(11)-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 31 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: O87696 (Residues: 1-242; Coverage: 93%)
Gene name: cbiF
Sequence domains: Tetrapyrrole (Corrin/Porphyrin) Methylases
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P3121
Unit cell:
a: 80.7Å b: 80.7Å c: 109.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.247
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
4 more

11 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
10 more