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(Cont.) In B. subtilis, the FGAR-AT is composed of three proteins: PurS, PurQ, and small PurL. The first characterization of the B. subtilis FGAR-AT complex was carried out, and it was determined that a complex between the three proteins can only be isolated in the presence of Mg2+-ADP and glutamine. By analogy to the Salmonella FGAR-AT, ADP is believed to be acting as a structural cofactor, while formation of a PurQ-glutamine complex is essential for assembly of the FGAR-AT. Subsequent biophysical studies have indicated that the physiologically relevant form of the FGAR-AT complex contains 2 PurS, 1 PurQ, and 1 small PurL. Further studies on PurQ have identified residues important for catalysis and complex formation, while insight into the small PurL active site has been obtained by studies on the T. maritima enzyme. The FGAR-AT complex provides a new system in purine biosynthesis to study metabolite transfer among weakly interacting proteins.

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