› 5fau

X-ray diffraction
1.9Å resolution

wild-type choline TMA lyase in complex with choline

Released:
DOI: 10.2210/pdb5fau/pdb
PDB entry 5fau coloured by chain, front view.
PDB entry 5fau coloured by chain, side view.
PDB entry 5fau coloured by chain, top view.
Source organism: Oleidesulfovibrio alaskensis G20
Primary publication:
Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase.
Bodea S, Funk MA, Balskus EP, Drennan CL
Cell Chem Biol 23 1206-1216 (2016)
PMID: 27642068

Function and Biology Details

Reaction catalysed: 
Choline = trimethylamine + acetaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174246 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Choline trimethylamine-lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 849 amino acids
Theoretical weight: 95 KDa
Source organism: Oleidesulfovibrio alaskensis G20
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q30W70 (Residues: 19-846; Coverage: 98%)
Gene names: Dde_3282, cutC
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

2 bound ligands:
Ligand CHT 4 x CHT
Ligand GOL 8 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 79.607Å b: 234.871Å c: 104.994Å
α: 90° β: 109.62° γ: 90°
R-values:
R R work R free
0.146 0.145 0.169
Expression system: Escherichia coli BL21(DE3)

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Citations

9 review citations

Chemical transformation of xenobiotics by the human gut microbiota.
Koppel et al. (2017)
8 more

12 mentions without citation

New tricks for the glycyl radical enzyme family.
Backman et al. (2017)
11 more