Biochemical and structural analysis of aminoglycoside acetyltransferase Eis from Anabaena variabilis

Rachel E. Pricer, Jacob L. Houghton, Keith D. Green, Abdelrahman S. Mayhoub, Sylvie Garneau-Tsodikova

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


The Mycobacterium tuberculosis enhanced intracellular survival (Eis-Mtb) protein is a clinically important aminoglycoside (AG) multi-acetylating enzyme. Eis homologues are found in a variety of mycobacterial and non-mycobacterial species. Variation of the residues lining the AG-binding pocket and positions of the loops bearing these residues in the Eis homologues dictates the substrate specificity and, thus, Eis homologues are Nature-made tools for elucidating principles of AG recognition by Eis. Here, we demonstrate that the Eis from Anabaena variabilis (Eis-Ava), the first non-mycobacterial Eis homologue reported, is a multi-acetylating AG-acetyltransferase. Eis-Ava, Eis from Mycobacterium tuberculosis (Eis-Mtb), and Eis from Mycobacterium smegmatis (Eis-Msm) have different structures of their AG-binding pockets. We perform comparative analysis of these differences and investigate how they dictate the substrate and cosubstrate recognition and acetylation of AGs by Eis.

Original languageEnglish
Pages (from-to)3305-3313
Number of pages9
JournalMolecular BioSystems
Issue number12
StatePublished - Dec 2012

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology


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