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

FEBS Letters

Liljas, Lars¹  Abdulkarim, Farhad¹  Hughes, Diarmaid¹ 

[1] Department of Molecular Biology, Box 590, The Biomedical Center, Uppsala University, Uppsala S-751 24, Sweden

关键词: EF-Tu;    Kirromycin;    Protein structure;    tuf mutation;    Salmonella typhimurium;    Escherichia coli;   

DOI  :  10.1016/0014-5793(94)00937-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 seven different 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 the mutations cluster on each side of the interface between domains I and III. We propose that this domain interface is the binding site for kirromycin.

【 授权许可】

Unknown