1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coliReport as inadecuate




1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli - Download this document for free, or read online. Document in PDF available to download.

Biomolecular NMR Assignments

, Volume 6, Issue 2, pp 163–167

First Online: 30 November 2011Received: 11 August 2011Accepted: 09 November 2011

Abstract

Viability and pathogenicity of Gram-negative bacteria is linked to the cytochrome c maturation and the oxidative protein folding systems in the periplasm. The transmembrane reductant conductor DsbD is a unique protein which provides the necessary reducing power to both systems through thiol-disulfide exchange reactions in a complex network of protein–protein interactions. The N-terminal domain of DsbD nDsbD is the delivery point of the reducing power originating from cytoplasmic thioredoxin to a variety of periplasmic partners. Here we report H, C and N assignments for resonances of nDsbD in its oxidized and reduced states. These assignments provide the starting point for detailed investigations of the interactions of nDsbD with its protein partners.

KeywordsEscherichia coli DsbD NMR resonance assignments Thiol:disulfide exchange reaction Oxidation-reduction Oxidoreductase  Download fulltext PDF



Author: Despoina A. I. Mavridou - Lukas S. Stelzl - Stuart J. Ferguson - Christina Redfield

Source: https://link.springer.com/







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