› 6eei

X-ray diffraction
1.99Å resolution

Crystal structure of Arabidopsis thaliana phenylacetaldehyde synthase in complex with L-phenylalanine

Released:
DOI: 10.2210/pdb6eei/pdb
PDB entry 6eei coloured by chain, front view.
PDB entry 6eei coloured by chain, side view.
PDB entry 6eei coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural basis for divergent and convergent evolution of catalytic machineries in plant aromatic amino acid decarboxylase proteins.
Torrens-Spence MP, Chiang YC, Smith T, Vicent MA, Wang Y, Weng JK
Proc Natl Acad Sci U S A 117 10806-10817 (2020)
PMID: 32371491

Function and Biology Details

Reactions catalysed: 
L-dopa + O(2) + H(2)O = 3,4-dihydroxyphenylacetaldehyde + CO(2) + NH(3) + H(2)O(2)
L-phenylalanine + O(2) + H(2)O = phenylacetaldehyde + CO(2) + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186059 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylacetaldehyde synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 490 amino acids
Theoretical weight: 54.71 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8RY79 (Residues: 1-490; Coverage: 100%)
Gene names: AADC, AAS, At2g20340, ELI5, F11A3.11
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand PHE 2 x PHE
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 78.064Å b: 106.791Å c: 115.903Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.205 0.24
Expression system: Escherichia coli

Quick links

Citations

5 review citations

General and specialized tyrosine metabolism pathways in plants.
Xu et al. (2020)
4 more

2 mentions without citation

Structural basis for divergent and convergent evolution of catalytic machineries in plant aromatic amino acid decarboxylase proteins.
Torrens-Spence et al. (2020)
1 more