4BWV

Structure of Adenosine 5-prime-phosphosulfate Reductase apr-b from Physcomitrella Patens

Summary for 4BWV

• Entry DOI: 10.2210/pdb4bwv/pdb
• Descriptor: PHOSPHOADENOSINE-PHOSPHOSULPHATE REDUCTASE, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: oxidoreductase, sulfate assimilation, sulfonucleotide
• Biological source: PHYSCOMITRELLA PATENS
• Total number of polymer chains: 2
• Total formula weight: 64424.55

Authors

Stevenson, C.E.M.,Hughes, R.K.,McManus, M.T.,Lawson, D.M.,Kopriva, S. (deposition date: 2013-07-04, release date: 2013-11-27, Last modification date: 2023-12-20)

Primary citation

Stevenson, C.E.M.,Hughes, R.K.,Mcmanus, M.T.,Lawson, D.M.,Kopriva, S.
The X-Ray Crystal Structure of Apr-B, an Atypical Adenosine 5-Prime-Phosphosulfate Reductase from Physcomitrella Patens
FEBS Lett., 587:3626-, 2013

PubMed 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.

PubMed: 24100135
DOI: 10.1016/J.FEBSLET.2013.09.034

Experimental method

X-RAY DIFFRACTION (1.8 Å)