1DKU

CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.

Summary for 1DKU

• Entry DOI: 10.2210/pdb1dku/pdb
• Related: 1DKR
• Descriptor: PROTEIN (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE), PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, METHYL PHOSPHONIC ACID ADENOSINE ESTER, ... (4 entities in total)
• Functional Keywords: open alpha-beta structure, domain duplication, phosphoribosyltransferase type i fold, transferase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm : P14193
• Total number of polymer chains: 2
• Total formula weight: 71361.40

Authors

Eriksen, T.A.,Kadziola, A.,Bentsen, A.-K.,Harlow, K.W.,Larsen, S. (deposition date: 1999-12-08, release date: 2000-04-05, Last modification date: 2024-02-07)

Primary citation

Eriksen, T.A.,Kadziola, A.,Bentsen, A.K.,Harlow, K.W.,Larsen, S.
Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase.
Nat.Struct.Biol., 7:303-308, 2000

PubMed Abstract: 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.

PubMed: 10742175
DOI: 10.1038/74069

Experimental method

X-RAY DIFFRACTION (2.2 Å)