› 1djq

X-ray diffraction
2.2Å resolution

STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF RECOMBINANT C30A MUTANT OF TRIMETHYLAMINE DEHYDROGENASE FROM METHYLOPHILUS METHYLOTROPHUS (SP. W3A1)

Released:
DOI: 10.2210/pdb1djq/pdb
PDB entry 1djq coloured by chain, front view.
PDB entry 1djq coloured by chain, side view.
PDB entry 1djq coloured by chain, top view.
Source organism: Methylophilus methylotrophus W3A1
Primary publication:
Structural and biochemical characterization of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from methylophilus methylotrophus (sp. W(3)A(1)).
Trickey P, Basran J, Lian LY, Chen Z, Barton JD, Sutcliffe MJ, Scrutton NS, Mathews FS
Biochemistry 39 7678-88 (2000)
PMID: 10869173

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:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147609 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trimethylamine dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 729 amino acids
Theoretical weight: 81.57 KDa
Source organism: Methylophilus methylotrophus W3A1
Expression system: Escherichia coli
UniProt:
  • Canonical: P16099 (Residues: 2-730; Coverage: 100%)
Gene name: tmd
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 148.09Å b: 72Å c: 83.76Å
α: 90° β: 97.77° γ: 90°
R-values:
R R work R free
0.139 0.139 0.187
Expression system: Escherichia coli

Quick links

Citations

2 review citations

A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes.
Sutcliffe et al. (2002)
1 more

3 mentions without citation

PoSSuM: a database of similar protein-ligand binding and putative pockets.
Ito et al. (2012)
2 more