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Article

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

The Journal of biological chemistry - 17 Jun 2011

Ticu Cristina, Murataliev Marat, Nechifor Roxana, Wilson Kevin S

Abstract excerpt

The antibiotic fusidic acid potently inhibits bacterial translation (and cellular growth) by lodging between domains I and III of elongation factor G (EF-G) and preventing release of EF-G from the ribosome. We examined the functions of key amino acid residues near the active site of EF-G that interact with fusidic acid and regulate hydrolysis of GTP. Alanine mutants of these residues spontaneously hydrolyzed GTP...

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Share to Guanosine Triphosphate

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

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Share to Peptide Elongation Factor G

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Share to Translocation, Genetic

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Identifiers

PMID: 21531717
DOI: 10.1074/jbc.M110.214056
PMCID: PMC3122226

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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.

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