› 1nth

X-ray diffraction
1.55Å resolution

Crystal structure of the methanosarcina barkeri monomethylamine methyltransferase (MTMB)

Released:
DOI: 10.2210/pdb1nth/pdb
PDB entry 1nth coloured by chain, front view.
PDB entry 1nth coloured by chain, side view.
PDB entry 1nth coloured by chain, top view.
Source organism: Methanosarcina barkeri
Primary publication:
A new UAG-encoded residue in the structure of a methanogen methyltransferase.
Hao B, Gong W, Ferguson TK, James CM, Krzycki JA, Chan MK
Science 296 1462-6 (2002)
PMID: 12029132

Function and Biology Details

Reaction catalysed: 
Methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monomethylamine methyltransferase MtmB1 Chain: A
Molecule details ›
Chain: A
Length: 458 amino acids
Theoretical weight: 50.29 KDa
Source organism: Methanosarcina barkeri
UniProt:
  • Canonical: O30642 (Residues: 1-458; Coverage: 100%)
Gene names: mtmB, mtmB1
Sequence domains: Monomethylamine methyltransferase MtmB
Structure domains: Monomethylamine methyltransferase MtmB

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P6322
Unit cell:
a: 158.464Å b: 158.464Å c: 135.797Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.176 0.188

Quick links

Citations

68 review citations

Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation.
Ragsdale et al. (2008)
67 more

2 mentions without citation

Discordant and chameleon sequences: their distribution and implications for amyloidogenicity.
Gendoo et al. (2011)
1 more