› 4obu

X-ray diffraction
2.8Å resolution

Ruminococcus gnavus tryptophan decarboxylase RUMGNA_01526 (apo)

Released:
DOI: 10.2210/pdb4obu/pdb
PDB entry 4obu coloured by chain, front view.
PDB entry 4obu coloured by chain, side view.
PDB entry 4obu coloured by chain, top view.
Source organism: [Ruminococcus] gnavus ATCC 29149
Primary publication:
Discovery and characterization of gut microbiota decarboxylases that can produce the neurotransmitter tryptamine.
Williams BB, Van Benschoten AH, Cimermancic P, Donia MS, Zimmermann M, Taketani M, Ishihara A, Kashyap PC, Fraser JS, Fischbach MA
Cell Host Microbe 16 495-503 (2014)
PMID: 25263219

Function and Biology Details

Reaction catalysed: 
L-tryptophan = tryptamine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan decarboxylase Chains: A, B, C, E, F, G, H, U
Molecule details ›
Chains: A, B, C, E, F, G, H, U
Length: 490 amino acids
Theoretical weight: 55.02 KDa
Source organism: [Ruminococcus] gnavus ATCC 29149
Expression system: Escherichia coli
UniProt:
  • Canonical: A7B1V0 (Residues: 1-490; Coverage: 100%)
Gene name: RUMGNA_01526
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PLP 8 x PLP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P1
Unit cell:
a: 58.63Å b: 145.77Å c: 165.07Å
α: 72.85° β: 88.84° γ: 88.3°
R-values:
R R work R free
0.232 0.231 0.257
Expression system: Escherichia coli

Quick links

Citations

157 review citations

Interactions between the microbiota, immune and nervous systems in health and disease.
Fung et al. (2017)
156 more

5 mentions without citation

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
4 more