› 4ab7

X-ray diffraction
3.25Å resolution

Crystal structure of a tetrameric acetylglutamate kinase from Saccharomyces cerevisiae complexed with its substrate N- acetylglutamate

Released:
DOI: 10.2210/pdb4ab7/pdb
PDB entry 4ab7 coloured by chain, front view.
PDB entry 4ab7 coloured by chain, side view.
PDB entry 4ab7 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase.
de Cima S, Gil-Ortiz F, Crabeel M, Fita I, Rubio V
PLoS One 7 e34734 (2012)
PMID: 22529931

Function and Biology Details

Reactions catalysed: 
N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169537 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylglutamate kinase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 464 amino acids
Theoretical weight: 51.34 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q01217 (Residues: 58-513; Coverage: 53%)
Gene names: ARG5,6, YER069W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NLG 2 x NLG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P1
Unit cell:
a: 92.883Å b: 103.269Å c: 111.313Å
α: 77.31° β: 89.27° γ: 70.43°
R-values:
R R work R free
0.195 0.193 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Synthetic metabolons for metabolic engineering.
Singleton et al. (2014)
1 more

2 mentions without citation

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