› 1ao0

X-ray diffraction
2.8Å resolution

GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE FROM B. SUBTILIS COMPLEXED WITH ADP AND GMP

Released:
DOI: 10.2210/pdb1ao0/pdb
PDB entry 1ao0 coloured by chain, front view.
PDB entry 1ao0 coloured by chain, side view.
PDB entry 1ao0 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.
Chen S, Tomchick DR, Wolle D, Hu P, Smith JL, Switzer RL, Zalkin H
Biochemistry 36 10718-26 (1997)
PMID: 9271502

Function and Biology Details

Reaction catalysed: 
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidophosphoribosyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 459 amino acids
Theoretical weight: 49.88 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P00497 (Residues: 12-470; Coverage: 96%)
Gene names: BSU06490, purF
Sequence domains: Glutamine amidotransferase domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 4 x MG
Ligand SF4 4 x SF4
Ligand 5GP 4 x 5GP
Ligand ADP 4 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 160.3Å b: 70.4Å c: 182.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.264
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
5 more

2 mentions without citation

Hysteretic and graded responses in bacterial two-component signal transduction.
Igoshin et al. (2008)
1 more