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

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

The Journal of biological chemistry - 13 Jan 2006

Xu Zhiqiang, O'Rourke Brendon A, Skurray Ronald A, Brown Melissa H

Abstract excerpt

The staphylococcal multidrug exporter QacA confers resistance to a wide range of structurally dissimilar monovalent and bivalent cationic antimicrobial compounds. To understand the functional importance of transmembrane segment 10, which is thought to be involved in substrate binding, cysteine-scanning mutagenesis was performed in which 35 amino acid residues in the putative transmembrane helix and its flanking...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Cysteine
Share to Drug Resistance, Multiple

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

Share to Maleimides

Share to Methionine

Share to Microscopy, Fluorescence

Share to Solvents

Share to Staphylococcus aureus

Source

Identifiers

PMID: 16282328
DOI: 10.1074/jbc.M508676200

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

Role of transmembrane segment 10 in efflux mediated by the staphylococcal multidrug transport protein QacA.PMID 16282328Read ↗

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 ↗

Active Export Proteins Mediating Drug Resistance in StaphylococciSemantic proximity Read ↗

Multidrug Transport by the ABC Transporter Sav1866 from <i>Staphylococcus aureus</i>Semantic proximity Read ↗

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

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

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

Decreased function of the class B tetracycline efflux protein Tet with mutations at aspartate 15, a putative intramembrane residue.Semantic proximity Read ↗

Extramembrane central pore of multidrug exporter AcrB in Escherichia coli plays an important role in drug transport.Semantic proximity Read ↗

Plasmid-Mediated Resistance to Thrombin-Induced Platelet Microbicidal Protein in Staphylococci: Role of the qacA LocusSemantic proximity Read ↗

Mutational analysis of polar amino acid residues within predicted transmembrane helices 10 and 16 of multidrug resistance protein 1 (ABCC1): effect on substrate specificity.Semantic proximity Read ↗

Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump.Semantic proximity Read ↗

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