2i2x

X-ray diffraction
2.5Å resolution

Crystal structure of methanol:cobalamin methyltransferase complex MtaBC from Methanosarcina barkeri

Released:

Function and Biology Details

Reaction catalysed:
Methanol + a [Co(I) methanol-specific corrinoid protein] = a [methyl-Co(III) methanol-specific corrinoid protein] + H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-175179 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Methanol--corrinoid protein co-methyltransferase Chains: A, C, E, G, I, K, M, O
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 461 amino acids
Theoretical weight: 50.85 KDa
Source organism: Methanosarcina barkeri
UniProt:
  • Canonical: Q46EH3 (Residues: 1-461; Coverage: 100%)
Gene names: Mbar_A0741, mtaB
Sequence domains: Methanol-cobalamin methyltransferase B subunit
Methanol--corrinoid protein Chains: B, D, F, H, J, L, N, P
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 258 amino acids
Theoretical weight: 27.88 KDa
Source organism: Methanosarcina barkeri
UniProt:
  • Canonical: Q46EH4 (Residues: 1-258; Coverage: 100%)
Gene names: Mbar_A0740, mtaC
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4, MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 101.75Å b: 172.85Å c: 190.54Å
α: 90° β: 98.86° γ: 90°
R-values:
R R work R free
0.184 0.182 0.231