› 2bty

X-ray diffraction
2.75Å resolution

Acetylglutamate kinase from Thermotoga maritima complexed with its inhibitor arginine

Released:
DOI: 10.2210/pdb2bty/pdb
PDB entry 2bty coloured by chain, front view.
PDB entry 2bty coloured by chain, side view.
PDB entry 2bty coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa.
Ramón-Maiques S, Fernández-Murga ML, Gil-Ortiz F, Vagin A, Fita I, Rubio V
J Mol Biol 356 695-713 (2006)
PMID: 16376937

Function and Biology Details

Reaction catalysed: 
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194885 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylglutamate kinase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 282 amino acids
Theoretical weight: 30.39 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X2A4 (Residues: 1-282; Coverage: 100%)
Gene names: TM_1784, argB
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

3 bound ligands:
Ligand ARG 3 x ARG
Ligand NLG 3 x NLG
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 94.998Å b: 207.709Å c: 117.996Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.242 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Surprising arginine biosynthesis: a reappraisal of the enzymology and evolution of the pathway in microorganisms.
Xu et al. (2007)
6 more

8 mentions without citation

The PII-NAGK-PipX-NtcA Regulatory Axis of Cyanobacteria: A Tale of Changing Partners, Allosteric Effectors and Non-covalent Interactions.
Forcada-Nadal et al. (2018)
7 more