The X-ray crystal structure of APR-B, an atypical adenosine 5′-phosphosulfate reductase from Physcomitrella patens

DOI: 10.1016/j.febslet.2013.09.034
PMID: 24100135

Authors: Clare Stevenson (John Innes Centre) , Richard Hughes (Department of Biological Chemistry, John Innes Centre, Colney Lane, Norwich) , Michael T. Mcmanus (Massey University) , David Lawson (John Innes Centre) , Stanislav Kopriva (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters

State: Published (Approved)
Published: October 2013

Abstract: We solved the structure of the first eukaryotic sulfonucleotide reductase. The plant enzyme is highly similar to its bacterial homologues on a subunit level. The PpAPR-B displays a novel quaternary structure

Journal Keywords: Amino; Bryopsida; Catalytic; Conserved; Crystallography; X-Ray; Kinetics; Models; Molecular; Oxidoreductases; Plant; Protein; Secondary; Structural; Protein; Substrate Specificity

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Added On: 15/10/2013 13:50

Discipline Tags:

Plant science Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)