› 1re5

X-ray diffraction
2.6Å resolution

Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida

Released:
DOI: 10.2210/pdb1re5/pdb
PDB entry 1re5 coloured by chain, front view.
PDB entry 1re5 coloured by chain, side view.
PDB entry 1re5 coloured by chain, top view.
Source organism: Pseudomonas putida KT2440
Primary publication:
Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways.
Yang J, Wang Y, Woolridge EM, Arora V, Petsko GA, Kozarich JW, Ringe D
Biochemistry 43 10424-34 (2004)
PMID: 15301541

Function and Biology Details

Reaction catalysed: 
2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = cis,cis-butadiene-1,2,4-tricarboxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate lyase C-terminal domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 450 amino acids
Theoretical weight: 48.25 KDa
Source organism: Pseudomonas putida KT2440
Expression system: Escherichia coli
UniProt:
  • Canonical: Q88N37 (Residues: 1-450; Coverage: 100%)
Gene names: PP_1379, pcaB
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand DTT 2 x DTT
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P65
Unit cell:
a: 231.523Å b: 231.523Å c: 78.456Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.212 0.242
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Stereochemistry of enzymatic water addition to C=C bonds.
Chen et al. (2015)
14 other articles

1 mention without citation

Anomalies in the vibrational dynamics of proteins are a consequence of fractal-like structure.
Reuveni et al. (2010)