The X‐ray crystal structure of APR‐B, an atypical adenosine 5′‐phosphosulfate reductase from Physcomitrella patens. Issue 22 (4th October 2013)

• Record Type: Journal Article
• Authors: Stevenson, Clare E.M.; Hughes, Richard K.; McManus, Michael T.; Lawson, David M.; Kopriva, Stanislav
• Is Part Of: FEBS letters. Volume 587:Issue 22(2013)
• Page Start: 3626
• Page End: 3632
• Publication Date: 2013-10-04
• Subjects: APS -- adenosine-5′-phosphosulfate -- APR -- adenosine-5′-phosphosulfate reductase -- PAPS -- 3′-phosphoadenosine-5′-phosphosulfate -- DLS -- dynamic light scattering -- ASU -- asymmetric unit -- Sulfate assimilation -- APS reductase -- X-ray structure -- Sulfonucleotide -- Physcomitrella patens; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.09.034
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Sulfonucleotide reductases catalyse the first reductive step of sulfate assimilation. Their substrate specificities generally correlate with the requirement for a [Fe4 S4 ] 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. Abstract : We solved the structure of the first eukaryotic sulfonucleotide reductase. The plant enzyme is highly similar to its bacterial homologues on a subunit level. The PpAPR‐B displays a novel quaternary structure.