Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP

• The antibiotic kirromycin inhibits protein synthesis by binding to EF-Tu and preventing its release from the ribosome after GTP hydrolysis.We have isolated and sequenced a collection of kirromycin resistant tuf mutations and identified thirteen single amino acid substitutions at sevendifferent sites in EF-Tu. These have been mapped onto the 3D structures of EF-Tu’GTP and EF-Tu.GDP. In the active GTP form of EF-Tu themutations cluster on each side of the interface between domains I and III. We propose that this domain interface is the binding site for kirromycin.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Microbiology in the medical area (hsv//eng)

Nyckelord

EF-Tu

Kirromycin

Protein structure

tgf mutation

Salmonella typhimurium

Escherichia coli

Microbiology, immunology, infectious diseases

Mikrobiologi, immunologi, infektionssjukdomar

Publikations- och innehållstyp

ref (ämneskategori)

art (ämneskategori)