{Reference Type}: Journal Article
{Title}: The X-ray crystal structure of APR-B, an atypical adenosine 5'-phosphosulfate reductase from Physcomitrella patens.
{Author}: Stevenson CE;Hughes RK;McManus MT;Lawson DM;Kopriva S;
{Journal}: FEBS Lett
{Volume}: 587
{Issue}: 22
{Year}: Nov 2013 15
{Factor}: 3.864
{DOI}: 10.1016/j.febslet.2013.09.034
{Abstract}: Sulfonucleotide reductases catalyse the first reductive step of sulfate assimilation. Their substrate specificities generally correlate with the requirement for a [Fe4S4] cluster, where adenosine 5'-phosphosulfate (APS) reductases possess a cluster and 3'-phosphoadenosine 5'-phosphosulfate reductases do not. The exception is the APR-B isoform of APS reductase from the moss Physcomitrella patens, which lacks a cluster. The crystal structure of APR-B, the first for a plant sulfonucleotide reductase, is consistent with a preference for APS. Structural conservation with bacterial APS reductase rules out a structural role for the cluster, but supports the contention that it enhances the activity of conventional APS reductases.