› 2v27

X-ray diffraction
1.5Å resolution

Structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H

Released:
DOI: 10.2210/pdb2v27/pdb
PDB entry 2v27 coloured by chain, front view.
PDB entry 2v27 coloured by chain, side view.
PDB entry 2v27 coloured by chain, top view.
Source organism: Colwellia psychrerythraea 34H
Primary publication:
Structure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability.
Leiros HK, Pey AL, Innselset M, Moe E, Leiros I, Steen IH, Martinez A
J Biol Chem 282 21973-86 (2007)
PMID: 17537732

Function and Biology Details

Reaction catalysed: 
L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine-4-hydroxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 275 amino acids
Theoretical weight: 31.81 KDa
Source organism: Colwellia psychrerythraea 34H
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q47XN7 (Residues: 1-267; Coverage: 100%)
Gene names: CPS_3766, phhA
Sequence domains: Biopterin-dependent aromatic amino acid hydroxylase
Structure domains: Aromatic amino acid hydroxylase

Ligands and Environments

2 bound ligands:
Ligand FE 2 x FE
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 40.28Å b: 86.02Å c: 87.57Å
α: 90° β: 97.01° γ: 90°
R-values:
R R work R free
0.164 0.162 0.195
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Some like it cold: understanding the survival strategies of psychrophiles.
De Maayer et al. (2014)
6 more

4 mentions without citation

Psychrophilic enzymes: from folding to function and biotechnology.
Feller G. (2013)
3 more