1dku
From Proteopedia
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CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.
Overview
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.
About this Structure
1DKU is a Single protein structure of sequence from Bacillus subtilis with AP2 and ABM as ligands. Active as Ribose-phosphate diphosphokinase, with EC number 2.7.6.1 Full crystallographic information is available from OCA.
Reference
Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase., Eriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S, Nat Struct Biol. 2000 Apr;7(4):303-8. PMID:10742175
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