› 4mlj

X-ray diffraction
2.3Å resolution

dihydrodipicolinate synthase from C. jejuni, Y110F mutation with pyruvate bound to the active site

Released:
DOI: 10.2210/pdb4mlj/pdb
PDB entry 4mlj coloured by chain, front view.
PDB entry 4mlj coloured by chain, side view.
PDB entry 4mlj coloured by chain, top view.
Source organism: Campylobacter jejuni
Primary publication:
Tyrosine 110 plays a critical role in regulating the allosteric inhibition of Campylobacter jejuni dihydrodipicolinate synthase by lysine.
Conly CJ, Skovpen YV, Li S, Palmer DR, Sanders DA
Biochemistry 53 7396-406 (2014)
PMID: 25369463

Function and Biology Details

Reaction catalysed: 
Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192936 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 306 amino acids
Theoretical weight: 33.74 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9PPB4 (Residues: 1-298; Coverage: 100%)
Gene names: Cj0806, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand PGE 2 x PGE
Ligand PG4 1 x PG4
Ligand EDO 1 x EDO
1 modified residue:
Ligand KPI 4 x KPI

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 80.61Å b: 97.24Å c: 148.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.141 0.2
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Kinetic, spectral, and structural studies of the slow-binding inhibition of the Escherichia coli dihydrodipicolinate synthase by 2, 4-oxo-pentanoic acid.
Karsten et al. (2021)
2 more