In this study, the X-ray crystal structures of APS kinase domains from human PAPS synthase were determined, showing the dynamic substrate recognition and a regulatory redox switch similar to plant APS kinases.
The sulfate donor 3'-phosphoadenosine-5'-phosphosulfate (PAPS) is a near-universal component of sulfur metabolism. In a report by Zhang et al. in this issue of Structure, X-ray crystal structures of the APS kinase domains from human PAPS synthase reveal dynamic substrate recognition and a regulatory redox switchanalogous to that previously described only in plant APS kinases.
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