HN, N, Cα and Cβ assignments of the two periplasmic domains of Neisseria meningitidis DsbD

DsbD is a disulfide bond reductase present in the inner membrane of many Gamma-Proteobacteria. In the human pathogen Neisseria meningitidis , DsbD is required for viability and represents a potential target for the development of antibiotics. Here we report the chemical shift assignments (H N , N, C α and C β ) for the reduced and oxidized forms of the two periplasmic domains of N. meningitidis DsbD, n- Nm DsbD and c- Nm DsbD. The backbone amide resonances in all four forms were completely assigned, and the secondary structures for the core regions of the proteins were calculated using 13 C αβ shifts. The reduced and oxidized forms of each domain have similar secondary shifts suggesting they retain the same fold. We anticipate that these data will provide an important basis for studying the interaction between n- Nm DsbD and c- Nm DsbD, which is required for electron transfer across the bacterial cytoplasmic membrane.