› 3d2m

X-ray diffraction
2.21Å resolution

Crystal structure of N-acetylglutamate synthase from Neisseria gonorrhoeae complexed with coenzyme A and L-glutamate

Released:
DOI: 10.2210/pdb3d2m/pdb
PDB entry 3d2m coloured by chain, front view.
PDB entry 3d2m coloured by chain, side view.
PDB entry 3d2m coloured by chain, top view.
Source organism: Neisseria gonorrhoeae
Primary publication:
Mechanism of allosteric inhibition of N-acetyl-L-glutamate synthase by L-arginine.
Min L, Jin Z, Caldovic L, Morizono H, Allewell NM, Tuchman M, Shi D
J Biol Chem 284 4873-80 (2009)
PMID: 19095660

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 COA 1 x COA
1 bound ligand:
Ligand GLU 1 x GLU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P312
Unit cell:
a: 98.802Å b: 98.802Å c: 90.107Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.229 0.28
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

NRPSs and amide ligases producing homopoly(amino acid)s and homooligo(amino acid)s.
Hamano et al. (2013)
1 more

6 mentions without citation

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