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

Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM4- siderophore analogues of varied linker length.

Scientific reports - 6 Apr 2017

Wilde Ellis J, Hughes Adam, Blagova Elena V, Moroz Olga V, Thomas Ross P, Turkenburg Johan P, Raines Daniel J, Duhme-Klair Anne-Kathrin, Wilson Keith S

Abstract excerpt

Bacteria use siderophores to mediate the transport of essential Fe(III) into the cell. In Campylobacter jejuni the periplasmic binding protein CeuE, an integral part of the Fe(III) transport system, has adapted to bind tetradentate siderophores using a His and a Tyr side chain to complete the Fe(III) coordination. A series of tetradentate siderophore mimics was synthesized in which the length of the linker...

Read the complete abstract on PubMed

Topics

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

Share to Campylobacter jejuni
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ferric Compounds

Share to Iron-Binding Proteins

Share to Periplasm

Share to Periplasmic Binding Proteins

Share to Siderophores

Share to Spermidine

Source

Open in PubMed Open full text

Identifiers

PMID: 28383577
DOI: 10.1038/srep45941
PMCID: PMC5382913

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAM4- siderophore analogues of varied linker length.PMID 28383577Read ↗

Bacteria in an intense competition for iron: Key component of the Campylobacter jejuni iron uptake system scavenges enterobactin hydrolysis product.Semantic proximity Read ↗

Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni.Semantic proximity Read ↗

Conformational rearrangements in the N-domain of Escherichia coli FepA during ferric enterobactin transport.Semantic proximity Read ↗

Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.Semantic proximity Read ↗

The Cys78-Asn88 loop region of the Campylobacter jejuni CstII is essential for α2,3-sialyltransferase activity: analysis of the His85 mutants.Semantic proximity Read ↗

A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB.Semantic proximity Read ↗

Cofacial heme binding is linked to dimerization by a bacterial heme transport protein.Semantic proximity Read ↗

Probing the heme-binding site of the cytochrome c maturation protein CcmE.Semantic proximity Read ↗

19F NMR studies provide insights into lipid membrane interactions of listeriolysin O, a pore forming toxin from Listeria monocytogenes.Semantic proximity Read ↗

The C-terminal flexible domain of the heme chaperone CcmE is important but not essential for its function.Semantic proximity Read ↗

Monomerization alters the dynamics of the lid region in Campylobacter jejuni CstII: an MD simulation study.Semantic proximity Read ↗

Structural insights into incorporation of norbornene amino acids for click modification of proteins.Semantic proximity Read ↗

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