› 4lnf

X-ray diffraction
2.95Å resolution

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-Q

Released:
DOI: 10.2210/pdb4lnf/pdb
PDB entry 4lnf coloured by chain, front view.
PDB entry 4lnf coloured by chain, side view.
PDB entry 4lnf coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism.
Murray DS, Chinnam N, Tonthat NK, Whitfill T, Wray LV, Fisher SH, Schumacher MA
J Biol Chem 288 35801-11 (2013)
PMID: 24158439

Function and Biology Details

Reaction catalysed: 
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146161 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 443 amino acids
Theoretical weight: 50.21 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P12425 (Residues: 2-444; Coverage: 100%)
Gene names: BSU17460, glnA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 36 x MG
Ligand GLN 12 x GLN
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P1
Unit cell:
a: 112Å b: 137.5Å c: 137.7Å
α: 119.8° β: 90.3° γ: 93.4°
R-values:
R R work R free
0.201 0.194 0.259
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Polyamine and Ethanolamine Metabolism in Bacteria as an Important Component of Nitrogen Assimilation for Survival and Pathogenicity.
Krysenko et al. (2022)
2 more

2 mentions without citation

Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism.
Murray et al. (2013)
1 more