› 1v9a

X-ray diffraction
2Å resolution

Crystal structure of Uroporphyrin-III C-methyl transferase from Thermus thermophilus complexed with S-adenyl homocysteine

Released:
DOI: 10.2210/pdb1v9a/pdb
PDB entry 1v9a coloured by chain, front view.
PDB entry 1v9a coloured by chain, side view.
PDB entry 1v9a coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus.
Rehse PH, Kitao T, Tahirov TH
Acta Crystallogr D Biol Crystallogr 61 913-9 (2005)
PMID: 15983414

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
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-178088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
uroporphyrinogen-III C-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 239 amino acids
Theoretical weight: 26.14 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SKH6 (Residues: 2-240; Coverage: 100%)
Gene name: TTHA0667
Sequence domains: Tetrapyrrole (Corrin/Porphyrin) Methylases
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 59.982Å b: 63.81Å c: 132.422Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Immunoproteomic analysis of outer membrane proteins and extracellular proteins of Actinobacillus pleuropneumoniae JL03 serotype 3.
Liao et al. (2009)
1 more

2 mentions without citation

Crystal structure of the heme d1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferases.
Storbeck et al. (2011)
1 more