› 3ab2

X-ray diffraction
2.59Å resolution

Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with threonine

Released:
DOI: 10.2210/pdb3ab2/pdb
PDB entry 3ab2 coloured by chain, front view.
PDB entry 3ab2 coloured by chain, side view.
PDB entry 3ab2 coloured by chain, top view.
Source organism: Corynebacterium glutamicum
Primary publication:
Mechanism of concerted inhibition of alpha2beta2-type hetero-oligomeric aspartate kinase from Corynebacterium glutamicum.
Yoshida A, Tomita T, Kuzuyama T, Nishiyama M
J Biol Chem 285 27477-27486 (2010)
PMID: 20573952

Function and Biology Details

Reaction catalysed: 
ATP + L-aspartate = ADP + 4-phospho-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150763 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartokinase Chains: A, C, E, G, I, K, M, O
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 421 amino acids
Theoretical weight: 44.8 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26512 (Residues: 1-421; Coverage: 100%)
Gene names: Cgl0251, cg0306, lysC
Sequence domains:
Structure domains:
Aspartokinase Chains: B, D, F, H, J, L, N, P
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 178 amino acids
Theoretical weight: 19.38 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26512 (Residues: 250-421; Coverage: 41%)
  • Best match: P26512-2 (Residues: 1-172)
Gene names: Cgl0251, cg0306, lysC
Sequence domains: ACT domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand THR 15 x THR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P1
Unit cell:
a: 101.833Å b: 119.093Å c: 124.384Å
α: 71.85° β: 69.48° γ: 72.72°
R-values:
R R work R free
0.234 0.232 0.28
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Structure, function, and regulation of enzymes involved in amino acid metabolism of bacteria and archaea.
Tomita T. (2017)
16 other articles

4 mentions without citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)
3 more