› 2q9h

X-ray diffraction
2.3Å resolution

Crystal structure of the C73S mutant of diaminopimelate epimerase

Released:
DOI: 10.2210/pdb2q9h/pdb
PDB entry 2q9h coloured by chain, front view.
PDB entry 2q9h coloured by chain, side view.
PDB entry 2q9h coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase.
Pillai B, Cherney M, Diaper CM, Sutherland A, Blanchard JS, Vederas JC, James MN
Biochem Biophys Res Commun 363 547-53 (2007)
PMID: 17889830

Function and Biology Details

Reaction catalysed: 
LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate
Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diaminopimelate epimerase Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 30.26 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P44859 (Residues: 1-274; Coverage: 100%)
Gene names: HI_0750, dapF
Sequence domains: Diaminopimelate epimerase
Structure domains: Diaminopimelate Epimerase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand TLA 1 x TLA
Ligand ACY 2 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2221
Unit cell:
a: 100.91Å b: 114.047Å c: 66.777Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.24
Expression system: Escherichia coli

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Citations

1 review citation

Enabling Role of Ligand-Driven Conformational Changes in Enzyme Evolution.
Richard JP. (2022)
11 other articles

1 mention without citation

Structural basis for redox sensitivity in Corynebacterium glutamicum diaminopimelate epimerase: an enzyme involved in l-lysine biosynthesis.
Sagong et al. (2017)