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

Structural insights into fusidic acid resistance and sensitivity in EF-G.

Journal of molecular biology - 13 May 2005

Hansson Sebastian, Singh Ranvir, Gudkov Anatoly T, Liljas Anders, Logan Derek T

Abstract excerpt

Fusidic acid (FA) is a steroid antibiotic commonly used against Gram positive bacterial infections. It inhibits protein synthesis by stalling elongation factor G (EF-G) on the ribosome after translocation. A significant number of the mutations conferring strong FA resistance have been mapped at the interfaces between domains G, III and V of EF-G. However, direct information on how such mutations affect the...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Drug Resistance, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Diphosphate

Share to Guanosine Triphosphate

Share to Lysine

Share to Peptide Elongation Factor G

Share to Structure-Activity Relationship

Share to Thermus thermophilus

Source

Identifiers

PMID: 15843024
DOI: 10.1016/j.jmb.2005.02.066

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

Structural insights into fusidic acid resistance and sensitivity in EF-G.PMID 15843024Read ↗

Staphylococcus aureus elongation factor G--structure and analysis of a target for fusidic acid.Semantic proximity Read ↗

Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid.Semantic proximity Read ↗

Mechanism of Elongation Factor-G-mediated Fusidic Acid Resistance and Fitness Compensation in Staphylococcus aureusSemantic proximity Read ↗

Structures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentaneSemantic proximity Read ↗

Structures of the <i>Staphylococcus aureus</i> ribosome inhibited by fusidic acid and fusidic acid cyclopentaneSemantic proximity Read ↗

A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistanceSemantic proximity Read ↗

A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation.Semantic proximity Read ↗

Detuning of the Ribosome Conformational Landscape Promotes Antibiotic Resistance and Collateral SensitivitySemantic proximity Read ↗

Molecular analysis of fusidic acid resistance in Staphylococcus aureusSemantic proximity Read ↗

Specific glycine-dependent enzyme motion determines the potency of conformation selective inhibitors of threonyl-tRNA synthetase.Semantic proximity Read ↗

Fusidic acid resistance through changes in the dynamics of the drug targetSemantic proximity Read ↗

Alterations in the peptidyltransferase and decoding domains of ribosomal RNA suppress mutations in the elongation factor G gene.Semantic proximity Read ↗

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