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1H, 13C and 15N backbone and side-chain chemical shift assignments for oxidized and reduced desulfothioredoxin

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Abstract

Based on sequence homology, desulfothioredoxin (DTrx) from Desulfovibrio vulgaris Hildenborough has been identified as a new member of the thioredoxin superfamily. Desulfothioredoxin (104 amino acids) contains a particular active site consensus sequence, CPHC probably correlated to the anaerobic metabolism of these bacteria. We report the full 1H, 13C and 15N resonance assignments of the reduced and the oxidized form of desulfothioredoxin (DTrx). 2D and 3D heteronuclear NMR experiments were performed using uniformly 15N-, 13C-labelled DTrx. More than 98% backbone and 96% side-chain 1H, 13C and 15N resonance assignments were obtained. (BMRB deposits with accession number 16712 and 16713).

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Authors and Affiliations

  1. IMR-IFR88, CNRS, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France

    Edwige B. Garcin, Olivier Bornet, Laetitia Pieulle, Françoise Guerlesquin & Corinne Sebban-Kreuzer

  2. Université de Provence, 3 place Victor Hugo, 13331, Marseille Cedex 3, France

    Edwige B. Garcin, Olivier Bornet, Laetitia Pieulle, Françoise Guerlesquin & Corinne Sebban-Kreuzer

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  1. Edwige B. Garcin
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  2. Olivier Bornet
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  3. Laetitia Pieulle
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  4. Françoise Guerlesquin
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  5. Corinne Sebban-Kreuzer
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Correspondence to Corinne Sebban-Kreuzer.

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Garcin, E.B., Bornet, O., Pieulle, L. et al. 1H, 13C and 15N backbone and side-chain chemical shift assignments for oxidized and reduced desulfothioredoxin. Biomol NMR Assign 4, 135–137 (2010). https://doi.org/10.1007/s12104-010-9226-9

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  • DOI: https://doi.org/10.1007/s12104-010-9226-9

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