› 2r8v

X-ray diffraction
2.5Å resolution

Native structure of N-acetylglutamate synthase from Neisseria gonorrhoeae

Released:
DOI: 10.2210/pdb2r8v/pdb
PDB entry 2r8v coloured by chain, front view.
PDB entry 2r8v coloured by chain, side view.
PDB entry 2r8v coloured by chain, top view.
Source organism: Neisseria gonorrhoeae
Primary publication:
The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation.
Shi D, Sagar V, Jin Z, Yu X, Caldovic L, Morizono H, Allewell NM, Tuchman M
J Biol Chem 283 7176-84 (2008)
PMID: 18184660

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amino-acid acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 49.24 KDa
Source organism: Neisseria gonorrhoeae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5FAK7 (Residues: 1-436; Coverage: 100%)
Gene names: NGO_0027, argA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P312
Unit cell:
a: 98.661Å b: 98.661Å c: 89.755Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.252
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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

5 mentions without citation

N-acetylglutamate synthase: structure, function and defects.
Caldovic et al. (2010)
4 more