› 2w37

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THE HEXAMERIC CATABOLIC ORNITHINE TRANSCARBAMYLASE FROM Lactobacillus hilgardii

Released:
DOI: 10.2210/pdb2w37/pdb
PDB entry 2w37 coloured by chain, front view.
PDB entry 2w37 coloured by chain, side view.
PDB entry 2w37 coloured by chain, top view.
Source organism: Lentilactobacillus hilgardii
Primary publication:
Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: Structural insights into the oligomeric assembly and metal binding.
de Las Rivas B, Fox GC, Angulo I, Ripoll MM, Rodríguez H, Muñoz R, Mancheño JM
J Mol Biol 393 425-34 (2009)
PMID: 19666033

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184467 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine carbamoyltransferase, catabolic Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 359 amino acids
Theoretical weight: 40.13 KDa
Source organism: Lentilactobacillus hilgardii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8G998 (Residues: 1-343; Coverage: 100%)
Gene name: arcB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

1 bound ligand:
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P321
Unit cell:
a: 156.805Å b: 156.805Å c: 80.623Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.244
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Sources and Fates of Carbamyl Phosphate: A Labile Energy-Rich Molecule with Multiple Facets.
Shi et al. (2018)
1 more

4 mentions without citation

Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways.
Medvedev et al. (2019)
3 more