› 1f38

X-ray diffraction
2.4Å resolution

X-RAY CRYSTALLOGRAPHIC STRUCTURE OF PRECORRIN 8W DECARBOXYLASE, THE PRODUCT OF GENE MT0146 IN THE METHANOBACTERIUM THERMOAUTOTROPHICUM GENOME

Released:
DOI: 10.2210/pdb1f38/pdb
PDB entry 1f38 coloured by chain, front view.
PDB entry 1f38 coloured by chain, side view.
PDB entry 1f38 coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.
Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF
Structure 10 1475-87 (2002)
PMID: 12429089

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + cobalt-precorrin-6B = S-adenosyl-L-homocysteine + cobalt-precorrin-7 + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127824 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 192 amino acids
Theoretical weight: 21.11 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O26249 (Residues: 1-192; Coverage: 100%)
Gene names: MTH_146, cbiT
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21212
Unit cell:
a: 74.47Å b: 194.76Å c: 59.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.291
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

2 mentions without citation

Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation.
Miller et al. (2010)
1 more