Back to article: Aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase AAC(6’)-Im

FIGURE 1: Sequence alignment of AAC(6’)-Im and AAC(6’)-Ie. The secondary structure assignment for AAC(6’)-Im is shown above, and the identity (*) and similarity (:) is indicated below each block of sequence. Amino acids involved in kanamycin A binding are shaded blue for those which are common to both enzymes, red for amino acids which interact with kanamycin A only in AAC(6’)-Im, and yellow for amino acids which interact with kanamycin A only in AAC(6’)-Ie [12]. The AAC(6’)-Im enzyme is one residue shorter than AAC(6’)-Ie, so for the sake of simplicity, the AAC(6’)-Im sequence numbering begins at Met2 so that the sequence numbering is the same for both enzymes.

[12] Smith CA, Toth M, Weiss TM, Frase H, Vakulenko SB (2014). Structure of the bifunctional aminoglycoside-resistance enzyme AAC(6′)-Ie-APH(2″)-Ia revealed by crystallographic and small-angle X-ray scattering analysis. Acta Crystallogr D70(10): 2754–2764.

By continuing to use the site, you agree to the use of cookies. more information

The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this. Please refer to our "privacy statement" and our "terms of use" for further information.