aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase aac(6’)-im

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ID: 155713
2017
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Abstract
Aminoglycoside 6’-acetyltransferase-Im (AAC(6’)-Im) is the closest monofunctional homolog of the AAC(6’)-Ie acetyltransferase of the bifunctional enzyme AAC(6’)-Ie/APH(2”)-Ia. The AAC(6’)-Im acetyltransferase confers 4- to 64-fold higher MICs to 4,6-disubstituted aminoglycosides and the 4,5-disubstituted aminoglycoside neomycin than AAC(6’)-Ie, yet unlike AAC(6’)-Ie, the AAC(6’)-Im enzyme does not confer resistance to the atypical aminoglycoside fortimicin. The structure of the kanamycin A complex of AAC(6’)-Im shows that the substrate binds in a shallow positively-charged pocket, with the N6’ amino group positioned appropriately for an efficient nucleophilic attack on an acetyl-CoA cofactor. The AAC(6’)-Ie enzyme binds kanamycin A in a sufficiently different manner to position the N6’ group less efficiently, thereby reducing the activity of this enzyme towards the 4,6-disubstituted aminoglycosides. Conversely, docking studies with fortimicin in both acetyltransferases suggest that the atypical aminoglycoside might bind less productively in AAC(6’)-Im, thus explaining the lack of resistance to this molecule.
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smith2017microbialaminoglycoside Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Clyde A. Smith, Monolekha Bhattacharya, Marta Toth, Nichole K. Stewart, Sergei B. Vakulenko
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Journal povolžskaâ arheologiâ
Year 2017
DOI
10.15698/mic2017.12.602
URL
http://microbialcell.com/researcharticles/aminoglycoside-resistance-profile-and-structural-architecture-of-the-aminoglycoside-acetyltransferase-aac6-im/
Keywords
antibiotic resistance aminoglycosides acetyltransferase crystal structurebiology (general)

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