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

Abstract

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
Volume11
Issue number2
DOIs
Publication statusPublished - 1 Oct 2017

Keywords

  • DsbD
  • Bacterial reductase
  • Disulfide reduction
  • Neisseria meningitidis

Cite this

@article{3ec85a18eadb4763bbf0269b46aca2da,
title = "HN, N, Cα and Cβ assignments of the two periplasmic domains of Neisseria meningitidis DsbD",
abstract = "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.",
keywords = "DsbD , Bacterial reductase, Disulfide reduction, Neisseria meningitidis",
author = "Smith, {Roxanne P} and Biswaranjan Mohanty and Williams, {Martin L} and Scanlon, {Martin J} and Begona Heras",
year = "2017",
month = "10",
day = "1",
doi = "10.1007/s12104-017-9743-x",
language = "English",
volume = "11",
pages = "181–186",
journal = "Biomolecular NMR Assignments",
issn = "1874-2718",
publisher = "Springer-Verlag London Ltd.",
number = "2",

}

HN, N, Cα and Cβ assignments of the two periplasmic domains of Neisseria meningitidis DsbD. / Smith, Roxanne P; Mohanty, Biswaranjan; Williams, Martin L; Scanlon, Martin J; Heras, Begona.

In: Biomolecular NMR Assignments, Vol. 11, No. 2, 01.10.2017, p. 181–186.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - HN, N, Cα and Cβ assignments of the two periplasmic domains of Neisseria meningitidis DsbD

AU - Smith, Roxanne P

AU - Mohanty, Biswaranjan

AU - Williams, Martin L

AU - Scanlon, Martin J

AU - Heras, Begona

PY - 2017/10/1

Y1 - 2017/10/1

N2 - 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.

AB - 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.

KW - DsbD

KW - Bacterial reductase

KW - Disulfide reduction

KW - Neisseria meningitidis

UR - http://www.scopus.com/inward/record.url?scp=85020308613&partnerID=8YFLogxK

U2 - 10.1007/s12104-017-9743-x

DO - 10.1007/s12104-017-9743-x

M3 - Article

VL - 11

SP - 181

EP - 186

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

SN - 1874-2718

IS - 2

ER -