› 2vss

X-ray diffraction
2.22Å resolution

Wild-type Hydroxycinnamoyl-CoA hydratase lyase in complex with acetyl- CoA and vanillin

Released:
DOI: 10.2210/pdb2vss/pdb
PDB entry 2vss coloured by chain, front view.
PDB entry 2vss coloured by chain, side view.
PDB entry 2vss coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) with acetyl-CoA and vanillin gives insights into substrate specificity and mechanism.
Bennett JP, Bertin L, Moulton B, Fairlamb IJ, Brzozowski AM, Walton NJ, Grogan G
Biochem J 414 281-9 (2008)
PMID: 18479250

Function and Biology Details

Reaction catalysed: 
(1a) feruloyl-CoA + H(2)O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130663 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Hydroxycinnamoyl-CoA hydratase-lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 276 amino acids
Theoretical weight: 31.04 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69762 (Residues: 1-276; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:
Hydroxycinnamoyl-CoA hydratase-lyase Chain: E
Molecule details ›
Chain: E
Length: 276 amino acids
Theoretical weight: 31.02 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69762 (Residues: 1-276; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:
Hydroxycinnamoyl-CoA hydratase-lyase Chain: F
Molecule details ›
Chain: F
Length: 276 amino acids
Theoretical weight: 31.07 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69762 (Residues: 1-276; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACO 4 x ACO
Ligand V55 1 x V55
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 90.223Å b: 130.595Å c: 144.663Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Vanillin-bioconversion and bioengineering of the most popular plant flavor and its de novo biosynthesis in the vanilla orchid.
Gallage et al. (2015)
1 more

2 mentions without citation

Structural and biophysical characterization of BoxC from Burkholderia xenovorans LB400: a novel ring-cleaving enzyme in the crotonase superfamily.
Bains et al. (2009)
1 more