4.7 Editorial Material

A tale of two switches: Redox regulation of adenosine-5'-phosphosulfate kinase in humans and plants

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STRUCTURE
卷 31, 期 7, 页码 757-759

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CELL PRESS
DOI: 10.1016/j.str.2023.06.006

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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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