› 1tkk

X-ray diffraction
2.1Å resolution

The Structure of a Substrate-Liganded Complex of the L-Ala-D/L-Glu Epimerase from Bacillus subtilis

Released:
DOI: 10.2210/pdb1tkk/pdb
PDB entry 1tkk coloured by chain, front view.
PDB entry 1tkk coloured by chain, side view.
PDB entry 1tkk coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Evolution of enzymatic activities in the enolase superfamily: structure of a substrate-liganded complex of the L-Ala-D/L-Glu epimerase from Bacillus subtilis.
Klenchin VA, Schmidt DM, Gerlt JA, Rayment I
Biochemistry 43 10370-8 (2004)
PMID: 15301535

Function and Biology Details

Reaction catalysed: 
L-alanyl-D-glutamate = L-alanyl-L-glutamate
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-128547 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-Ala-D/L-Glu epimerase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 366 amino acids
Theoretical weight: 39.52 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O34508 (Residues: 1-366; Coverage: 100%)
Gene names: BSU12980, ykfB
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 8 x MG
Ligand ALA 8 x ALA
Ligand GLU 8 x GLU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 117.4Å b: 134.6Å c: 194.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.219 0.285
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan).
Park et al. (2008)
3 more

6 mentions without citation

The Enzyme Function Initiative.
Gerlt et al. (2011)
5 more