› 4r53

X-ray diffraction
2Å resolution

dihydrodipicolinate synthase from C. jejuni with vacant active site and vacant allosteric site

Released:
DOI: 10.2210/pdb4r53/pdb
PDB entry 4r53 coloured by chain, front view.
PDB entry 4r53 coloured by chain, side view.
PDB entry 4r53 coloured by chain, top view.
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
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: 33.7 KDa
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
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

5 bound ligands:
Ligand EDO 5 x EDO
Ligand PEG 2 x PEG
Ligand CL 2 x CL
Ligand PGE 3 x PGE
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P21
Unit cell:
a: 77.22Å b: 97.56Å c: 82.4Å
α: 90° β: 109.47° γ: 90°
R-values:
R R work R free
0.175 0.174 0.213
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway.
Schmitz et al. (2020)
2 more