› 3c1n

X-ray diffraction
2.72Å resolution

Crystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonine

Released:
DOI: 10.2210/pdb3c1n/pdb
PDB entry 3c1n coloured by chain, front view.
PDB entry 3c1n coloured by chain, side view.
PDB entry 3c1n coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
The structural basis for allosteric inhibition of a threonine-sensitive aspartokinase.
Liu X, Pavlovsky AG, Viola RE
J Biol Chem 283 16216-25 (2008)
PMID: 18334478

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable aspartokinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 473 amino acids
Theoretical weight: 51.46 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57991 (Residues: 1-473; Coverage: 100%)
Gene name: MJ0571
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand THR 7 x THR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 110.039Å b: 144.317Å c: 155.358Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.236 0.29
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism.
Lang et al. (2014)
1 more

3 mentions without citation

The structural basis for allosteric inhibition of a threonine-sensitive aspartokinase.
Liu et al. (2008)
2 more