Journal
FEBS LETTERS
Volume 587, Issue 22, Pages 3626-3632Publisher
WILEY
DOI: 10.1016/j.febslet.2013.09.034
Keywords
Sulfate assimilation; APS reductase; X-ray structure; Sulfonucleotide; Physcomitrella patens
Funding
- Biotechnology and Biological Sciences Research Council [BB/J004561/1]
- John Innes Foundation
- Diamond Light Source
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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. Crown Copyright (C) 2013 Published by Elsevier B.V. on behalf of Federation of European Biochemical Society. All rights reserved.
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