The X-ray crystal structure of APR-B, an atypical adenosine 5 %26apos;-phosphosulfate reductase from Physcomitrella patens

作者：Stevenson Clare E M; Hughes Richard K; McManus Michael T; Lawson David M; Kopriva Stanislav^*

来源：FEBS LETTERS, 2013, 587(22): 3626-3632.

DOI：10.1016/j.febslet.2013.09.034

• Sulfate assimilation
• APS reductase
• X-ray structure
• Sulfonucleotide
• Physcomitrella patens

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 %26apos;-phosphosulfate (APS) reductases possess a cluster and 3 %26apos;-phosphoadenosine 5%26apos;-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.

• 出版日期2013-11-15