› 5fay

X-ray diffraction
1.9Å resolution

Y208F mutant of choline TMA-lyase

Released:
DOI: 10.2210/pdb5fay/pdb
PDB entry 5fay coloured by chain, front view.
PDB entry 5fay coloured by chain, side view.
PDB entry 5fay 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
Molecule details ›
Chains: A, B
Length: 815 amino acids
Theoretical weight: 91.57 KDa
Source organism: Oleidesulfovibrio alaskensis G20
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q30W70 (Residues: 53-846; Coverage: 94%)
Gene names: Dde_3282, cutC
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

3 bound ligands:
Ligand NA 3 x NA
Ligand MLI 9 x MLI
Ligand CHT 2 x CHT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P42212
Unit cell:
a: 228.941Å b: 228.941Å c: 78.952Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.193
Expression system: Escherichia coli BL21(DE3)

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Citations

11 review citations

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

1 mention without citation

Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase.
Bodea et al. (2016)