› 1bkh

X-ray diffraction
2.1Å resolution

MUCONATE LACTONIZING ENZYME FROM PSEUDOMONAS PUTIDA

Released:
DOI: 10.2210/pdb1bkh/pdb
PDB entry 1bkh coloured by chain, front view.
PDB entry 1bkh coloured by chain, side view.
PDB entry 1bkh coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.
Hasson MS, Schlichting I, Moulai J, Taylor K, Barrett W, Kenyon GL, Babbitt PC, Gerlt JA, Petsko GA, Ringe D
Proc Natl Acad Sci U S A 95 10396-401 (1998)
PMID: 9724714

Function and Biology Details

Reaction catalysed: 
(+)-muconolactone = cis,cis-muconate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175993 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 369 amino acids
Theoretical weight: 39.88 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: Q51958 (Residues: 4-372; Coverage: 99%)
Gene name: catB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I422
Unit cell:
a: 136.18Å b: 136.18Å c: 265.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.157 not available
Expression system: Escherichia coli

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Citations

9 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
8 more

3 mentions without citation

Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.
Hasson et al. (1998)
2 more