Flipping the Switch “On” for Aminoglycoside-Resistance Enzymes: The Mechanism Is Finally Revealed!

Huy X. Ngo; Sylvie Garneau-Tsodikova

doi:10.1016/j.str.2016.06.006

Flipping the Switch “On” for Aminoglycoside-Resistance Enzymes: The Mechanism Is Finally Revealed!

Huy X. Ngo, Sylvie Garneau-Tsodikova

Research output: Contribution to journal › Short survey › peer-review

2 Scopus citations

Abstract

In a recent issue of Structure, Caldwell et al. (2016) determined crystal structures of APH(2″)-Ia in complex with various combinations of aminoglycosides and nucleosides, which compellingly revealed that the catalytic activity of this resistance enzyme is regulated by a conformational change of the triphosphate of GTP, a mechanism previously unknown for antibiotic kinases.

Original language	English
Pages (from-to)	1011-1013
Number of pages	3
Journal	Structure
Volume	24
Issue number	7
DOIs	https://doi.org/10.1016/j.str.2016.06.006
State	Published - 2016

Bibliographical note

Publisher Copyright:
© 2016 Elsevier Ltd

Funding

We apologize to colleagues working in the antibiotic resistance field whose work was not cited due to space limitations. Our work on aminoglycoside resistance is supported by a National Institute of Health (NIH) grant AI090048 (to S.G.-T.).

Funders	Funder number
National Institutes of Health (NIH)
National Institute of Allergy and Infectious Diseases	R01AI090048

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.str.2016.06.006

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abstract = "In a recent issue of Structure, Caldwell et al. (2016) determined crystal structures of APH(2″)-Ia in complex with various combinations of aminoglycosides and nucleosides, which compellingly revealed that the catalytic activity of this resistance enzyme is regulated by a conformational change of the triphosphate of GTP, a mechanism previously unknown for antibiotic kinases.",

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Flipping the Switch “On” for Aminoglycoside-Resistance Enzymes: The Mechanism Is Finally Revealed!

Abstract

Bibliographical note

Funding

ASJC Scopus subject areas

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