Solution Structure and Backbone Dynamics of the Cysteine 103 to Serine Mutant of the N-Terminal Domain of DsbD from Neisseria meningitides-Reference-Cited by-同舟云学术

Solution Structure and Backbone Dynamics of the Cysteine 103 to Serine Mutant of the N-Terminal Domain of DsbD from Neisseria meningitides

Published:2008-11-05 Issue:48 Volume:47 Page:12710-12720
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Quinternet Marc¹,Tsan Pascale¹,Selme Laure¹,Beaufils Chrystel¹,Jacob Christophe¹,Boschi-Muller Sandrine¹,Averlant-Petit Marie-Christine¹,Branlant Guy¹,Cung Manh-Thong¹

Affiliation:

1. Laboratoire de Chimie Physique Macromoléculaire, UMR 7568 CNRS-INPL, Nancy Université, 1 rue Grandville, B.P. 20451, 54001 Nancy cedex, France, and Maturation des ARN et Enzymologie Moléculaire, UMR 7567 CNRS-UHP, Nancy Université, Faculté des Sciences et Techniques, Bld des Aiguillettes, B.P. 239, 54506 Vandœuvre-lès-Nancy, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801343c

Reference48 articles.

1. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli

2. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm

3. Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function

4. Thiol−Disulfide Exchange in an Immunoglobulin-like Fold: Structure of the N-Terminal Domain of DsbD,

5. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex

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1. Molecular Mechanisms of the Methionine Sulfoxide Reductase System from Neisseria meningitidis;Antioxidants;2018-10-01

2. Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens;Journal of Biological Chemistry;2018-10

3. HN, N, Cα and Cβ assignments of the two periplasmic domains of Neisseria meningitidis DsbD;Biomolecular NMR Assignments;2017-06-06

4. Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability;Biochemical Journal;2015-05-22

5. Structural Plasticity of the Thioredoxin Recognition Site of Yeast Methionine S-Sulfoxide Reductase Mxr1;Journal of Biological Chemistry;2011-04