1H, 13C and 15N backbone and side-chain chemical shift assignments for reduced unusual thioredoxin Patrx2 of Pseudomonas aeruginosa. - Archive ouverte HAL Access content directly
Journal Articles Biomol NMR Assign Year : 2014

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

Abstract

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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hal-01458208 , version 1 (06-02-2017)

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Edwige B Garcin, Olivier Bornet, Latifa El Antak, Matthieu Nouailler, Francoise Guerlesquin, et al.. 1H, 13C and 15N backbone and side-chain chemical shift assignments for reduced unusual thioredoxin Patrx2 of Pseudomonas aeruginosa.. Biomol NMR Assign, 2014, 8 (2), pp.247--50. ⟨10.1007/s12104-013-9493-3⟩. ⟨hal-01458208⟩
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