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Article

Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy.

Journal of molecular biology - 20 Jul 2007

Mavridou Despoina A I, Stevens Julie M, Ferguson Stuart J, Redfield Christina

Abstract excerpt

The periplasmic C-terminal domain of the Escherichia coli DsbD protein (cDsbD) has a thioredoxin fold. The two cysteine residues in the CXXC motif serve as the reductant for the disulfide bond of the N-terminal domain which can in turn act as a reductant for various periplasmic partners. The resulting disulfide bond in cDsbD is reduced via an unknown mechanism by the transmembrane helical domain of the protein....

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Identifiers

PMID: 17544440
DOI: 10.1016/j.jmb.2007.04.038

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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