› 1j21

X-ray diffraction
2.2Å resolution

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with ATP and citrulline

Released:
DOI: 10.2210/pdb1j21/pdb
PDB entry 1j21 coloured by chain, front view.
PDB entry 1j21 coloured by chain, side view.
PDB entry 1j21 coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms: stereochemistry of the catalytic reaction.
Goto M, Omi R, Miyahara I, Sugahara M, Hirotsu K
J Biol Chem 278 22964-71 (2003)
PMID: 12684518

Function and Biology Details

Reaction catalysed: 
ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Argininosuccinate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 400 amino acids
Theoretical weight: 44.88 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P59846 (Residues: 1-400; Coverage: 100%)
Gene names: TTHA0284, argG
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 4 x ATP
Ligand CIR 4 x CIR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: R3
Unit cell:
a: 229.2Å b: 229.2Å c: 161.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.23 0.259
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Almost all about citrulline in mammals.
Curis et al. (2005)
3 more

1 mention without citation

Short and simple sequences favored the emergence of N-helix phospho-ligand binding sites in the first enzymes.
Longo et al. (2020)