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1H, 13C and 15N backbone and side-chain chemical shift assignments for reduced unusual thioredoxin Patrx2 of Pseudomonas aeruginosa.

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Garcin, Edwige B | Bornet, Olivier | El Antak, Latifa | Nouailler, Matthieu | Guerlesquin, Francoise | Sebban-Kreuzer, Corinne

Edité par CCSD -

International audience. The gram-negative organism Pseudomonas aeruginosa is an opportunistic human pathogen and a leading cause of hospital-acquired infections. In P. aeruginosa PAO1, three cytoplasmic thioredoxins have been identified. An unusual thioredoxin (Patrx2) (108 amino acids) encoded by the PA2694 gene, is identified as a new thioredoxin-like protein based on sequence homology. Thioredoxin is a ubiquitous protein, which serves as a general protein disulfide oxidoreductase. Patrx2 present an atypical active site CGHC. We report the nearly complete (1)H, (13)C and (15)N resonance assignments of reduced Patrx2. 2D and 3D heteronuclear NMR experiments were performed with uniformly (15)N-, (13)C-labelled Patrx2, resulting in 97.2% backbone and 92.5% side-chain (1)H, (13)C and (15)N resonance assignments for the reduced form. (BMRB deposits with accession number 18130).

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