Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues.

Journal of bacteriology - 1 Oct 2006

Hiniker Annie, Vertommen Didier, Bardwell James C A, Collet Jean-Francois

Abstract excerpt

The mechanism by which DsbD transports electrons across the cytoplasmic membrane is unknown. Here we provide evidence that DsbD's conformation depends on its oxidation state. Our data also suggest that four highly conserved prolines surrounding DsbD's membrane-embedded catalytic cysteines may hav...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Conserved Sequence
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Oxidation-Reduction

Share to Oxidoreductases

Share to Peptide Hydrolases

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 17015672
DOI: 10.1128/JB.00383-06
PMCID: PMC1636233

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17015672-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues.PMID 17015672Read ↗

Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade.Semantic proximity Read ↗

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

Role of cysteines in mammalian VDAC isoforms' function.Semantic proximity Read ↗

Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.Semantic proximity Read ↗

Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.Semantic proximity Read ↗

Identification of a segment of DsbB essential for its respiration-coupled oxidation.Semantic proximity Read ↗

Mutational analysis of the disulfide catalysts DsbA and DsbB.Semantic proximity Read ↗

Membrane topology and mutational analysis of Escherichia coli CydDC, an ABC-type cysteine exporter required for cytochrome assembly.Semantic proximity Read ↗

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Semantic proximity Read ↗

Snapshots of DsbA in action: detection of proteins in the process of oxidative folding.Semantic proximity Read ↗

Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.Semantic proximity Read ↗

Structural determinants of substrate access to the disulfide oxidase Erv2p.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.