› 1m5s

X-ray diffraction
1.85Å resolution

Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri

Released:
DOI: 10.2210/pdb1m5s/pdb
PDB entry 1m5s coloured by chain, front view.
PDB entry 1m5s coloured by chain, side view.
PDB entry 1m5s coloured by chain, top view.
Source organism: Methanosarcina barkeri
Primary publication:
Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.
Mamat B, Roth A, Grimm C, Ermler U, Tziatzios C, Schubert D, Thauer RK, Shima S
Protein Sci 11 2168-78 (2002)
PMID: 12192072

Function and Biology Details

Reaction catalysed: 
Formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157295 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formylmethanofuran--tetrahydromethanopterin formyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 297 amino acids
Theoretical weight: 31.7 KDa
Source organism: Methanosarcina barkeri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55301 (Residues: 1-297; Coverage: 100%)
Gene names: Mbar_A0980, ftr
Sequence domains:
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 127.1Å b: 83.8Å c: 126.4Å
α: 90° β: 108.4° γ: 90°
R-values:
R R work R free
0.197 0.197 0.248
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Orthogonal multipolar interactions in structural chemistry and biology.
Paulini et al. (2005)
3 more

2 mentions without citation

Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.
Mamat et al. (2002)
1 more