2.0 Å X‐ray structure of the ternary complex of 7,8‐dihydro‐6‐hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue

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Abstract
The X‐ray crystal structure of 7,8‐dihydro‐6‐hydroxymethylpterinpyrophosphokinase (PPPK) in a ternary complex with ATP and a pterin analogue has been solved to 2.0 Å resolution, giving, for the first time, detailed information of the PPPK/ATP intermolecular interactions and the accompanying conformational change. The first 100 residues of the 158 residue peptide contain a βαββαβ motif present in several other proteins including nucleoside diphosphate kinase. Comparative sequence examination of a wide range of prokaryotic and lower eukaryotic species confirms the conservation of the PPPK active site, indicating the value of this de novo folate biosynthesis pathway enzyme as a potential target for the development of novel broad‐spectrum anti‐infective agents.