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

Insights into stabilizing interactions in the distorted domain-swapped dimer of Salmonella typhimurium survival protein.

Acta crystallographica. Section D, Biological crystallography - 1 Sept 2015

Mathiharan Yamuna Kalyani, Savithri H S, Murthy M R N

Abstract excerpt

The survival protein SurE from Salmonella typhimurium (StSurE) is a dimeric protein that functions as a phosphatase. SurE dimers are formed by the swapping of a loop with a pair of β-strands and a C-terminal helix between two protomers. In a previous study, the Asp230 and His234 residues were mutated to Ala to abolish a hydrogen bond that was thought to be crucial for C-terminal helix swapping. These mutations...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Salmonella typhimurium

Source

Identifiers

PMID: 26327371
DOI: 10.1107/S1399004715011992

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into stabilizing interactions in the distorted domain-swapped dimer of Salmonella typhimurium survival protein.PMID 26327371Read ↗

Dramatic structural changes resulting from the loss of a crucial hydrogen bond in the hinge region involved in C-terminal helix swapping in SurE: a survival protein from Salmonella typhimurium.Semantic proximity Read ↗

The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima.Semantic proximity Read ↗

Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: dimer dissociation by disruption of Val-Leu knot.Semantic proximity Read ↗

Crystal structure of the periplasmic disulfide-bond isomerase DsbC from Salmonella enterica serovar Typhimurium and the mechanistic implications.Semantic proximity Read ↗

Destabilization of psychrotrophic RNase HI in a localized fashion as revealed by mutational and X-ray crystallographic analyses.Semantic proximity Read ↗

Remarkable stabilization of a psychrotrophic RNase HI by a combination of thermostabilizing mutations identified by the suppressor mutation method.Semantic proximity Read ↗

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

Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA.Semantic proximity Read ↗

Structural basis for the function of stringent starvation protein a as a transcription factor.Semantic proximity Read ↗

Identification of rare slipknots in proteins and their implications for stability and folding.Semantic proximity Read ↗

Crystal structure details of Vibrio fischeri DarR and mutant DarR-M202I from LTTR family reveals their activation mechanism.Semantic proximity Read ↗

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

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