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

Biochemical characterization of the multidrug regulator QacR distinguishes residues that are crucial to multidrug binding and induction of qacA transcription.

Biochemistry - 20 Oct 2009

Peters Kate M, Sharbeen George, Theis Torsten, Skurray Ronald A, Brown Melissa H

Abstract excerpt

Staphylococcus aureus transcription factor QacR regulates expression of the qacA multidrug efflux determinant. In response to binding cationic lipophilic compounds, including ethidium and rhodamine 6G, QacR dissociates from the qacA operator alleviating repression. Such ligand binding uniformly induces a coil-to-helix transition of residues Thr(89)-Tyr(93) revealing an asymmetric binding pocket in QacR containing...

Read the complete abstract on PubMed

Topics

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

Share to Drug Resistance, Microbial
Share to Ethidium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Homeostasis

Share to Ligands

Share to Membrane Transport Proteins

Share to Repressor Proteins

Share to Rhodamines

Share to Staphylococcus aureus

Source

Identifiers

PMID: 19761200
DOI: 10.1021/bi901102h

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

Biochemical characterization of the multidrug regulator QacR distinguishes residues that are crucial to multidrug binding and induction of qacA transcription.PMID 19761200Read ↗

Interactions of the QacR Multidrug-Binding Protein with Structurally Diverse Ligands: Implications for the Evolution of the Binding PocketSemantic proximity Read ↗

Structural and biochemical characterization of MepR, a multidrug binding transcription regulator of the Staphylococcus aureus multidrug efflux pump MepA.Semantic proximity Read ↗

Functional analyses reveal an important role for tyrosine residues in the staphylococcal multidrug efflux protein QacA.Semantic proximity Read ↗

Analysis of tryptophan residues in the staphylococcal multidrug transporter QacA reveals long-distance functional associations of residues on opposite sides of the membrane.Semantic proximity Read ↗

Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition.Semantic proximity Read ↗

Mutations within the mepA operator affect binding of the MepR regulatory protein and its induction by MepA substrates in Staphylococcus aureus.Semantic proximity Read ↗

Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance.Semantic proximity Read ↗

Functional consequences of substitution mutations in MepR, a repressor of the Staphylococcus aureus MepA multidrug efflux pump gene.Semantic proximity Read ↗

Role of transmembrane segment 10 in efflux mediated by the staphylococcal multidrug transport protein QacA.Semantic proximity Read ↗

Critical biophysical properties in the Pseudomonas aeruginosa efflux gene regulator MexR are targeted by mutations conferring multidrug resistance.Semantic proximity Read ↗

QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization.Semantic proximity Read ↗

The src homology 3-like domain of the diphtheria toxin repressor (DtxR) modulates repressor activation through interaction with the ancillary metal ion-binding site.Semantic proximity Read ↗

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