title: Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.
abstract: 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 beta sheet and differs from the interface of A- and B-Prx dimers, where proteins associate in the plane parallel to the beta 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.
authors.affiliation: LCM3B, Groupe Biocristallographie, Université Henri Poincaré-Nancy1, UMR CNRS 7036, 54506 Vandoeuvre, France.
authors.forename: Aude
authors.initials: A
authors.lastname: Echalier
authors.forename: Xavier
authors.initials: X
authors.lastname: Trivelli
authors.forename: Catherine
authors.initials: C
authors.lastname: Corbier
authors.forename: Nicolas
authors.initials: N
authors.lastname: Rouhier
authors.forename: Olivier
authors.initials: O
authors.lastname: Walker
authors.forename: Pascale
authors.initials: P
authors.lastname: Tsan
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Jacquot
authors.forename: André
authors.initials: A
authors.lastname: Aubry
authors.forename: Isabelle
authors.initials: I
authors.lastname: Krimm
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Lancelin
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D016384:Consensus Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D054477:Glutaredoxins; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism; D054464:Peroxiredoxins; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism; D032107:Populus / Q000201:enzymology*; D012996:Solutions; D013499:Surface Properties; D013816:Thermodynamics; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D054477:Glutaredoxins; D010940:Plant Proteins; D012996:Solutions; D013879:Thioredoxins; D010088:Oxidoreductases; D010544:Peroxidases; D054464:Peroxiredoxins