Structural highlights
Publication Abstract from PubMed
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.
The X-ray crystal structure of APR-B, an atypical adenosine 5'-phosphosulfate reductase from Physcomitrella patens.,Stevenson CE, Hughes RK, McManus MT, Lawson DM, Kopriva S FEBS Lett. 2013 Nov 15;587(22):3626-32. doi: 10.1016/j.febslet.2013.09.034. Epub , 2013 Oct 4. PMID:24100135[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stevenson CE, Hughes RK, McManus MT, Lawson DM, Kopriva S. The X-ray crystal structure of APR-B, an atypical adenosine 5'-phosphosulfate reductase from Physcomitrella patens. FEBS Lett. 2013 Nov 15;587(22):3626-32. doi: 10.1016/j.febslet.2013.09.034. Epub , 2013 Oct 4. PMID:24100135 doi:http://dx.doi.org/10.1016/j.febslet.2013.09.034
