Cover Picture: Chemical and Structural Insights into the Regioversatility of the Aminoglycoside Acetyltransferase Eis (ChemBioChem 16/2013). Issue 16 (25th October 2013)

• Record Type: Journal Article
• Authors: Houghton, Jacob L.; Biswas, Tapan; Chen, Wenjing; Tsodikov, Oleg V.; Garneau‐Tsodikova, Sylvie
• Is Part Of: Chembiochem. Volume 14:Issue 16(2013)
• Page Start: 2061
• Page End: 2061
• Publication Date: 2013-10-25
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201390058
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The cover picture shows</bold> how the Eis enzyme from <italic>Mycobacterium tuberculosis</italic> binds its substrate, aminoglycoside tobramycin, for acetylation. Acetylation of aminoglycosides by Eis causes resistance to these drugs in tuberculosis. On <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 2127 ff., </ext-link> O. V. Tsodikov, S. Garneau‐Tsodikova et al. reveal two new acetylation positions for this enzyme on aminoglycoside scaffolds: the 3′′‐amine of tobramycin, kanamycin, and amikacin as well as the γ‐amine of the 4‐amino‐2‐hydroxybutyryl group of amikacin. A cartoon of the crystal structure of the ternary complex of Eis, CoA, and tobramycin demonstrates that this aminoglycoside can bind Eis in two distinct conformations, one for acetylation of the 6′‐position (tobramycin in pink with the acetylation position in turquoise) and one for acetylation at the 3′′‐position (tobramycin in green with the acetylation position in lilac). <boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg4t78rnpf" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>