Saturation mutagenesis of TsrA Ala4 unveils a highly mutable residue of thiostrepton A.

Zhang, Feifei

Saturation mutagenesis of TsrA Ala4 unveils a highly mutable residue of thiostrepton A. [electronic resource] - ACS chemical biology Apr 2015 - 998-1009 p. digital

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.

1554-8937

10.1021/cb5007745 doi


Anti-Bacterial Agents--chemistry
Bacillus--drug effects
Drug Evaluation, Preclinical--methods
Enterococcus faecium--drug effects
Microbial Sensitivity Tests
Models, Molecular
Mutagenesis, Site-Directed
Proteasome Endopeptidase Complex--metabolism
Proteasome Inhibitors--chemistry
Protein Conformation
Protein Engineering--methods
Staphylococcus aureus--drug effects
Streptomyces--genetics
Thiostrepton--analogs & derivatives