› 5ltm

X-ray diffraction
2.41Å resolution

Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis (Y78F-C503S-C565S) bound to cinnamate

Released:
DOI: 10.2210/pdb5ltm/pdb
PDB entry 5ltm coloured by chain, front view.
PDB entry 5ltm coloured by chain, side view.
PDB entry 5ltm coloured by chain, top view.
Source organism: Anabaena
Primary publication:
Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes.
Weise NJ, Ahmed ST, Parmeggiani F, Galman JL, Dunstan MS, Charnock SJ, Leys D, Turner NJ
Sci Rep 7 13691 (2017)
PMID: 29057979

Function and Biology Details

Reaction catalysed: 
L-phenylalanine = trans-cinnamate + ammonia
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine ammonia-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 537 amino acids
Theoretical weight: 58.74 KDa
Source organism: Anabaena
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q3M5Z3 (Residues: 25-563; Coverage: 95%)
Gene name: Ava_3988
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand HCI 2 x HCI
1 modified residue:
Ligand MDO 2 x MDO

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P4322
Unit cell:
a: 78.077Å b: 78.077Å c: 354.492Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.206
Expression system: Escherichia coli BL21

Quick links

Citations

10 citation in other articles

The production of L- and D-phenylalanines using engineered phenylalanine ammonia lyases from Petroselinum crispum.
Tork et al. (2019)
9 more

3 mentions without citation

Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes.
Weise et al. (2017)
2 more