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

Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant.

Journal of molecular biology - 1 Apr 2005

Ondo-Mbele Etienne, Vivès Corinne, Koné Amadou, Serre Laurence

Abstract excerpt

Escherichia coli DsbA belongs to the thioredoxin family and catalyzes the formation of disulfide bonds during the folding of proteins in the bacterial periplasm. It active site (C30-P31-H32-C33) consists of a disulfide bridge that is transferred to newly translocated proteins. The work reported here refers to the DsbA mutant termed C33A that retains, towards reduced unfolded thrombin inhibitor, an activity...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Isomerism

Share to Molecular Structure

Share to Proline

Share to Protein Conformation

Share to Protein Disulfide-Isomerases

Source

Identifiers

PMID: 15755450
DOI: 10.1016/j.jmb.2005.01.049

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant.PMID 15755450Read ↗

Staphylococcus aureus DsbA Does Not Have a Destabilizing DisulfideSemantic proximity Read ↗

Conversion of a catalytic into a structural disulfide bond by circular permutation.Semantic proximity Read ↗

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

Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli.Semantic proximity Read ↗

Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB.Semantic proximity Read ↗

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

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

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Semantic proximity Read ↗

DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.Semantic proximity Read ↗

Solution structure and backbone dynamics of the cysteine 103 to serine mutant of the N-terminal domain of DsbD from Neisseria meningitidis.Semantic proximity Read ↗

Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli.Semantic proximity Read ↗

Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain.Semantic proximity Read ↗

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