Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP
1994 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 352, 118-122 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
1994. Vol. 352, 118-122 p.
EF-Tu, Kirromycin, Protein structure, tgf mutation, Salmonella typhimurium, Escherichia coli
Microbiology in the medical area
IdentifiersURN: urn:nbn:se:uu:diva-47251DOI: 10.1016/0014-5793(94)00937-6OAI: oai:DiVA.org:uu-47251DiVA: diva2:75158