1DKR: Crystal Structures Of Bacillus Subtilis Phosphoribosylpyrophosphate Synthetase: Molecular Basis Of Allosteric Inhibition And Activation

Here we report the first three-dimensional structure of a phosphoribosylpyrophosphate (PRPP) synthetase. PRPP is an essential intermediate in several biosynthetic pathways. Structures of the Bacillus subtilis PRPP synthetase in complex with analogs of the activator phosphate and the allosteric inhibitor ADP show that the functional form of the enzyme is a hexamer. The individual subunits fold into two domains, both of which resemble the type I phosphoribosyltransfereases. The active site is located between the two domains and includes residues from two subunits. Phosphate and ADP bind to the same regulatory site consisting of residues from three subunits of the hexamer. In addition to identifying residues important for binding substrates and effectors, the structures suggest a novel mode of allosteric regulation.
PDB ID: 1DKRDownload
MMDB ID: 12855
PDB Deposition Date: 1999/12/8
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1DKR: hexameric; determined by author and by software (PISA,PQS)
Molecular Components in 1DKR
Label Count Molecule
Proteins (6 molecules)
Phosphoribosyl Pyrophosphate Synthetase(Gene symbol: prs)
Molecule annotation
Chemicals (12 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB