› 3m4n

X-ray diffraction
1.9Å resolution

Crystal structure of N-acetyl-L-ornithine transcarbamylase K302A mutant complexed with PALAO

Released:
DOI: 10.2210/pdb3m4n/pdb
PDB entry 3m4n coloured by chain, front view.
PDB entry 3m4n coloured by chain, side view.
PDB entry 3m4n coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris
Primary publication:
Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase.
Li Y, Yu X, Ho J, Fushman D, Allewell NM, Tuchman M, Shi D
Biochemistry 49 6887-95 (2010)
PMID: 20695527

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + N(2)-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylornithine carbamoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 359 amino acids
Theoretical weight: 40.03 KDa
Source organism: Xanthomonas campestris pv. campestris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8P8J2 (Residues: 1-339; Coverage: 100%)
Gene names: XCC2249, argF'
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

2 bound ligands:
Ligand PA9 1 x PA9
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I213
Unit cell:
a: 128.917Å b: 128.917Å c: 128.917Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.198 0.232
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Beyond gene expression: the impact of protein post-translational modifications in bacteria.
Cain et al. (2014)
2 more

1 mention without citation

Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase.
Li et al. (2010)