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 ¹H, ¹³C and ¹⁵N resonance assignments of reduced Patrx2. 2D and 3D heteronuclear NMR experiments were performed with uniformly ¹⁵N-, ¹³C-labelled Patrx2, resulting in 97.2 % backbone and 92.5 % side-chain ¹H, ¹³C and ¹⁵N resonance assignments for the reduced form. (BMRB deposits with accession number 18130).