title: 1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough.
abstract: Thioredoxins are ubiquitous key antioxidant enzymes which play an essential role in cell defense against oxidative stress. They maintain the redox homeostasis owing to the regulation of thiol-disulfide exchange. In the present paper, we report the full resonance assignments of (1)H, (13)C and (15)N atoms for the reduced and oxidized forms of Desulfovibrio vulgaris Hildenborough thioredoxin 1 (Trx1). 2D and 3D heteronuclear NMR experiments were performed using uniformly (15)N-, (13)C-labelled Trx1. Chemical shifts of 97% of the backbone and 90% of the side chain atoms were obtained for the oxidized and reduced form (BMRB deposits with accession number 17299 and 17300, respectively).
authors.affiliation: IMR-IFR88, CNRS; Aix-Marseille Université, Marseille, France.
authors.forename: Edwige B
authors.initials: EB
authors.lastname: Garcin
authors.forename: Olivier
authors.initials: O
authors.lastname: Bornet
authors.forename: Laetitia
authors.initials: L
authors.lastname: Pieulle
authors.forename: Françoise
authors.initials: F
authors.lastname: Guerlesquin
authors.forename: Corinne
authors.initials: C
authors.lastname: Sebban-Kreuzer
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D016969:Desulfovibrio vulgaris / Q000737:chemistry*; D007554:Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000737:chemistry; D013879:Thioredoxins / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D007554:Isotopes; D011994:Recombinant Proteins; D013879:Thioredoxins