4BWV

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

4BWV の概要

• エントリーDOI: 10.2210/pdb4bwv/pdb
• 分子名称: PHOSPHOADENOSINE-PHOSPHOSULPHATE REDUCTASE, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: oxidoreductase, sulfate assimilation, sulfonucleotide
• 由来する生物種: PHYSCOMITRELLA PATENS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64424.55

構造登録者

Stevenson, C.E.M.,Hughes, R.K.,McManus, M.T.,Lawson, D.M.,Kopriva, S. (登録日: 2013-07-04, 公開日: 2013-11-27, 最終更新日: 2023-12-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)