› 1o95

X-ray diffraction
3.7Å resolution

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

Released:
DOI: 10.2210/pdb1o95/pdb
PDB entry 1o95 coloured by chain, front view.
PDB entry 1o95 coloured by chain, side view.
PDB entry 1o95 coloured by chain, top view.
Source organism: Methylophilus methylotrophus
Primary publication:
Extensive conformational sampling in a ternary electron transfer complex.
Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS
Nat Struct Biol 10 219-25 (2003)
PMID: 12567183

Function and Biology Details

Reaction catalysed: 
Trimethylamine + H(2)O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-147610 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Trimethylamine dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 729 amino acids
Theoretical weight: 81.61 KDa
Source organism: Methylophilus methylotrophus
UniProt:
  • Canonical: P16099 (Residues: 2-730; Coverage: 100%)
Gene name: tmd
Sequence domains:
Structure domains:
Electron transfer flavoprotein subunit beta Chains: C, E
Molecule details ›
Chains: C, E
Length: 264 amino acids
Theoretical weight: 28.93 KDa
Source organism: Methylophilus methylotrophus
Expression system: Escherichia coli
UniProt:
  • Canonical: P53570 (Residues: 1-264; Coverage: 100%)
Gene name: etfB
Sequence domains: Electron transfer flavoprotein domain
Structure domains: HUPs
Electron transfer flavoprotein subunit alpha Chains: D, F
Molecule details ›
Chains: D, F
Length: 320 amino acids
Theoretical weight: 33.62 KDa
Source organism: Methylophilus methylotrophus
Expression system: Escherichia coli
UniProt:
  • Canonical: P53571 (Residues: 2-321; Coverage: 100%)
Gene name: etfA
Sequence domains:
Structure domains: HUPs

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
3 bound ligands:
Ligand ADP 2 x ADP
Ligand SF4 2 x SF4
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 102.5Å b: 116.513Å c: 138.706Å
α: 90° β: 95.35° γ: 90°
R-values:
R R work R free
0.257 0.252 0.353
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Control of protein functional dynamics by peptide linkers.
Wriggers et al. (2005)
12 more