› 3dg6

X-ray diffraction
1.6Å resolution

Crystal structure of muconate lactonizing enzyme from Mucobacterium Smegmatis complexed with muconolactone

Released:
DOI: 10.2210/pdb3dg6/pdb
PDB entry 3dg6 coloured by chain, front view.
PDB entry 3dg6 coloured by chain, side view.
PDB entry 3dg6 coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes.
Sakai A, Fedorov AA, Fedorov EV, Schnoes AM, Glasner ME, Brown S, Rutter ME, Bain K, Chang S, Gheyi T, Sauder JM, Burley SK, Babbitt PC, Almo SC, Gerlt JA
Biochemistry 48 1445-53 (2009)
PMID: 19220063

Function and Biology Details

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-106313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 40.02 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
  • Canonical: A0QTN8 (Residues: 1-367; Coverage: 100%)
Gene name: MSMEG_1910
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand MUC 1 x MUC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: I422
Unit cell:
a: 123.84Å b: 123.84Å c: 117.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.201
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Directed evolution drives the next generation of biocatalysts.
Turner NJ. (2009)
6 more

3 mentions without citation

Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes.
Sakai et al. (2009)
2 more