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Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Molecular Biology.
1994 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 352, 118-122 p.Article in journal (Refereed) Published
Abstract [en]

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.
Keyword [en]
EF-Tu, Kirromycin, Protein structure, tgf mutation, Salmonella typhimurium, Escherichia coli
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:uu:diva-47251DOI: 10.1016/0014-5793(94)00937-6OAI: oai:DiVA.org:uu-47251DiVA: diva2:75158
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2017-12-05Bibliographically approved

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Hughes, Diarmaid

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