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

Roxanne P Smith, Biswaranjan Mohanty, Martin L Williams, Martin J Scanlon, Begona Heras

Research output: Contribution to journalArticleResearchpeer-review

1 Citation (Scopus)


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 (HN, N, Cα and Cβ) for the reduced and oxidized forms of the two periplasmic domains of N. meningitidis DsbD, n-NmDsbD and c-NmDsbD. 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 13Cαβ 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-NmDsbD and c-NmDsbD, which is required for electron transfer across the bacterial cytoplasmic membrane.
Original languageEnglish
Pages (from-to)181–186
Number of pages6
JournalBiomolecular NMR Assignments
Issue number2
Publication statusPublished - 1 Oct 2017


  • DsbD
  • Bacterial reductase
  • Disulfide reduction
  • Neisseria meningitidis

Cite this