Crystal Structure and Solution NMR Dynamics of a D (Type II) Peroxiredoxin Glutaredoxin and Thioredoxin Dependent:  A New Insight into the Peroxiredoxin Oligomerism

• Published in: Biochemistry (Easton) Vol. 44; no. 6; pp. 1755 - 1767
• Main Authors: Echalier, Aude, Trivelli, Xavier, Corbier, Catherine, Rouhier, Nicolas, Walker, Olivier, Tsan, Pascale, Jacquot, Jean-Pierre, Aubry, André, Krimm, Isabelle, Lancelin, Jean-Marc
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 15.02.2005
• Subjects: Amino Acid Sequence; Binding Sites; Biochemistry, Molecular Biology; Consensus Sequence; Crystallization; Crystallography, X-Ray; Dimerization; Glutaredoxins; Life Sciences; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular - methods; Oxidoreductases - chemistry; Oxidoreductases - metabolism; Peroxidases - chemistry; Peroxidases - metabolism; Peroxiredoxins; Plant Proteins - chemistry; Plant Proteins - metabolism; Populus - enzymology; Solutions; Surface Properties; Thermodynamics; Thioredoxins - chemistry; Thioredoxins - metabolism; NMR; RMN; THIOREDOXIN; PEROXIREDOXIN; CRYSTAL STRUCTURE; GLUTAREDOXIN; POPULUS TRICHOCARPA
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi048226s

Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine. Very abundant in all organisms, Prxs are produced as diverse isoforms characterized by different catalytic mechanisms and various thiol-containing reducing agents. The oligomeric state of Prxs and the link with their functionality is a subject of intensive research. We present here a combined X-ray and nuclear magnetic resonance (NMR) study of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus trichocarpa Prx is the first Prx shown to be regenerated in vitro by both the glutaredoxin and thioredoxin systems. The crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution. The dimer interface is roughly perpendicular to the plane of the central β sheet and differs from the interface of A- and B-Prx dimers, where proteins associate in the plane parallel to the β sheet. The homodimer interface involves residues strongly conserved in the D (type II) Prxs, suggesting that all Prxs of this family can homodimerize. The study provides a new insight into the Prx oligomerism and the basis for protein−protein and enzyme−substrate interaction studies by NMR.