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

The S2 Cu(i) site in CupA from Streptococcus pneumoniae is required for cellular copper resistance.

Metallomics : integrated biometal science - 1 Jan 2016

Fu Yue, Bruce Kevin E, Wu Hongwei, Giedroc David P

Abstract excerpt

Pathogenic bacteria have evolved copper homeostasis and resistance systems for fighting copper toxicity imposed by the human immune system. Streptococcus pneumoniae is a respiratory pathogen that encodes an obligatorily membrane-anchored Cu(i) binding protein, CupA, and a P1B-type ATPase efflux transporter, CopA. The soluble, cytoplasmic domain of CupA (sCupA) contains a binuclear Cu(i) cluster consisting of S1...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Copper
Share to Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Chaperones

Share to Mutant Proteins

Share to Protein Structure, Secondary

Share to Solutions

Share to Streptococcus pneumoniae

Source

Open in PubMed Open full text

Identifiers

PMID: 26346139
DOI: 10.1039/c5mt00221d
PMCID: PMC4720546

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The S2 Cu(i) site in CupA from Streptococcus pneumoniae is required for cellular copper resistance.PMID 26346139Read ↗

A new structural paradigm in copper resistance in Streptococcus pneumoniae.Semantic proximity Read ↗

Exploring the role of the various methionine residues in the <i>Escherichia coli</i> CusB adapter proteinSemantic proximity Read ↗

A Tetranuclear Cu(I) Cluster in the Metallochaperone Protein CopZSemantic proximity Read ↗

Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF.Semantic proximity Read ↗

PcoB is a defense outer membrane protein that facilitates cellular uptake of copperSemantic proximity Read ↗

Cu+-specific CopB transporter: Revising P1B-type ATPase classification.Semantic proximity Read ↗

Role of Glutathione in Buffering Excess Intracellular Copper in Streptococcus pyogenes.Semantic proximity Read ↗

A role for glutathione in buffering excess intracellular copper in <i>Streptococcus pyogenes</i>Semantic proximity Read ↗

<scp>AdcA</scp> and <scp>AdcAII</scp> employ distinct zinc acquisition mechanisms and contribute additively to zinc homeostasis in <scp><i>S</i></scp><i>treptococcus pneumoniae</i>Semantic proximity Read ↗

Identification and characterization of a Streptococcus pyogenes ABC transporter with multiple specificity for metal cationsSemantic proximity Read ↗

Prokaryotic Substrate-Binding Proteins as Targets for Antimicrobial TherapiesSemantic proximity Read ↗

Proteomic analysis of the copper resistance of Streptococcus pneumoniaeSemantic proximity Read ↗

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