4.7 Editorial Material

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

Journal

STRUCTURE
Volume 31, Issue 7, Pages 757-759

Publisher

CELL PRESS
DOI: 10.1016/j.str.2023.06.006

Keywords

-

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available