Abstract
The gene encoding the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase of Haemophilus influenzae has been cloned and expressed in Escherichia coli. A complex of the purified protein with a substrate analog has been crystallized and its structure solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethione-labeled protein. The enzyme folds into a four-stranded antiparallel β-sheet flanked on one side by two α-helices and on the other by three consecutive α-helices, giving a novel β1α1β2β3α2β4α3α4α5 polypeptide topology. The three-dimensional structure of a binary complex has been refined at 2.1 Å resolution. The location of the substrate analog and a sulfate ion gives important insight into the molecular mechanism of the enzyme.
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