The X-ray crystal structure of APR-B,an atypical adenosine 5′-phosphosulfate reductase from Physcomitrella patens |
| |
| Authors: | Clare EM Stevenson Richard K Hughes Michael T McManus David M Lawson Stanislav Kopriva |
| |
| Institution: | 1. Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK;2. Institute of Molecular BioSciences, Massey University, Private Bag 11222, Palmerston North, New Zealand;3. Department of Metabolic Biology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK |
| |
| Abstract: | 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. |
| |
| Keywords: | APS adenosine-5&prime -phosphosulfate APR adenosine-5&prime -phosphosulfate reductase PAPS 3&prime -phosphoadenosine-5&prime -phosphosulfate DLS dynamic light scattering ASU asymmetric unit |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
