4ay8

X-ray diffraction
2.1Å resolution

SeMet-derivative of a methyltransferase from M. mazei

Released:
Model geometry
Fit model/data
Source organism: Methanosarcina mazei
Primary publication:
Structure of the corrinoid:coenzyme M methyltransferase MtaA from Methanosarcina mazei.
Acta Crystallogr D Biol Crystallogr 68 1549-57 (2012)
PMID: 23090404

Function and Biology Details

Reaction catalysed:
A [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-185824 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uroporphyrinogen decarboxylase (URO-D) domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 348 amino acids
Theoretical weight: 37.74 KDa
Source organism: Methanosarcina mazei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8PXZ6 (Residues: 1-342; Coverage: 100%)
Gene names: MM_1070, mtaA
Sequence domains: Uroporphyrinogen decarboxylase (URO-D)
Structure domains: TIM Barrel

Ligands and Environments

2 modified residues:

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BESSY BEAMLINE 14.3
Spacegroup: P32
Unit cell:
a: 125.21Å b: 125.21Å c: 38.88Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.148 0.146 0.177
Expression system: Escherichia coli BL21(DE3)